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Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]

 FAS2_YEAST              Reviewed;        1887 AA.
P19097; D6W3D9; Q12533;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
15-MAY-2002, sequence version 2.
17-JUN-2020, entry version 214.
RecName: Full=Fatty acid synthase subunit alpha;
EC=2.3.1.86;
Includes:
RecName: Full=Acyl carrier;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
EC=1.1.1.100;
AltName: Full=Beta-ketoacyl reductase;
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
EC=2.3.1.41;
AltName: Full=Beta-ketoacyl synthase;
Name=FAS2; OrderedLocusNames=YPL231W; ORFNames=P1409;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2900835;
Mohamed A.H., Chirala S.S., Mody N.H., Huang W.Y., Wakil S.J.;
"Primary structure of the multifunctional alpha subunit protein of yeast
fatty acid synthase derived from FAS2 gene sequence.";
J. Biol. Chem. 263:12315-12325(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 26786 / X2180-1A;
Schueller H.-J.;
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
G3 (Bethesda) 4:389-398(2014).
[5]
MUTAGENESIS OF GLY-1250.
STRAIN=ATCC 204508 / S288c;
PubMed=8041367; DOI=10.1007/bf00280191;
Inokoshi J., Tomoda H., Hashimoto H., Watanabe A., Takeshima H., Omura S.;
"Cerulenin-resistant mutants of Saccharomyces cerevisiae with an altered
fatty acid synthase gene.";
Mol. Gen. Genet. 244:90-96(1994).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling
pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-958 AND SER-1440, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 76625 / YPH499;
PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
"Profiling phosphoproteins of yeast mitochondria reveals a role of
phosphorylation in assembly of the ATP synthase.";
Mol. Cell. Proteomics 6:1896-1906(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome
analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides insights
into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[13]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 671-1744 IN COMPLEX WITH FAS1, AND
SUBUNIT.
PubMed=17448991; DOI=10.1016/j.cell.2007.03.013;
Lomakin I.B., Xiong Y., Steitz T.A.;
"The crystal structure of yeast fatty acid synthase, a cellular machine
with eight active sites working together.";
Cell 129:319-332(2007).
[14]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH FAS1, SUBUNIT, AND
PHOSPHOPANTETHEINYLATION AT SER-180.
PubMed=17431182; DOI=10.1126/science.1138249;
Leibundgut M., Jenni S., Frick C., Ban N.;
"Structural basis for substrate delivery by acyl carrier protein in the
yeast fatty acid synthase.";
Science 316:288-290(2007).
[15]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) IN COMPLEX WITH FAS1 AND THE
INHIBITOR CERULENIN, AND ACTIVITY REGULATION.
PubMed=18725634; DOI=10.1073/pnas.0805827105;
Johansson P., Wiltschi B., Kumari P., Kessler B., Vonrhein C., Vonck J.,
Oesterhelt D., Grininger M.;
"Inhibition of the fungal fatty acid synthase type I multienzyme complex.";
Proc. Natl. Acad. Sci. U.S.A. 105:12803-12808(2008).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1766-1887 IN COMPLEX WITH FAS1 AND
ACETYL-COA, MUTAGENESIS OF VAL-1769; GLY-1770; VAL-1771; ASP-1772;
VAL-1773; GLU-1774; ARG-1841; VAL-1879 AND VAL-1881, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=19679086; DOI=10.1016/j.str.2009.06.014;
Johansson P., Mulinacci B., Koestler C., Vollrath R., Oesterhelt D.,
Grininger M.;
"Multimeric options for the auto-activation of the Saccharomyces cerevisiae
FAS type I megasynthase.";
Structure 17:1063-1074(2009).
-!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit
contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-
protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This
subunit coordinates the binding of the six beta subunits to the enzyme
complex.
-!- CATALYTIC ACTIVITY:
Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
ChEBI:CHEBI:83139; EC=2.3.1.86;
-!- CATALYTIC ACTIVITY:
Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
+ CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
EC=2.3.1.41;
-!- CATALYTIC ACTIVITY:
Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
+ NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
-!- ACTIVITY REGULATION: Inhibited by cerulenin by covalent binding to
active site of the ketoacyl synthase (KS) region.
{ECO:0000269|PubMed:18725634}.
-!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
(alpha and beta). {ECO:0000269|PubMed:17431182,
ECO:0000269|PubMed:17448991, ECO:0000269|PubMed:18725634,
ECO:0000269|PubMed:19679086}.
-!- INTERACTION:
P19097; P07149: FAS1; NbExp=8; IntAct=EBI-6806, EBI-6795;
-!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
of the Acyl carrier domain by the C-terminal PPT domain. This
modification is essential for activity because fatty acids are bound in
thioester linkage to the sulfhydryl of the prosthetic group.
-!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
synthetase subunit alpha family. {ECO:0000305}.
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EMBL; J03936; AAA34601.1; -; Genomic_DNA.
EMBL; X76890; CAA54218.1; -; Genomic_DNA.
EMBL; X94561; CAA64256.1; -; Genomic_DNA.
EMBL; Z73586; CAA97947.1; -; Genomic_DNA.
EMBL; Z73587; CAA97948.1; -; Genomic_DNA.
EMBL; BK006949; DAA11205.1; -; Genomic_DNA.
PIR; S61703; S61703.
RefSeq; NP_015093.1; NM_001184045.1.
PDB; 2ML8; NMR; -; A=138-302.
PDB; 2PFF; X-ray; 4.00 A; A/D/G=671-1744.
PDB; 2UV8; X-ray; 3.10 A; A/B/C=1-1887.
PDB; 2VKZ; X-ray; 4.00 A; A/B/C=1-1887.
PDB; 2WAS; X-ray; 1.90 A; A/B/C/D/E/F=1766-1887.
PDB; 2WAT; X-ray; 2.20 A; A/B/C/D/E/F=1766-1887.
PDB; 3HMJ; X-ray; 4.00 A; A/B/C=1-1887.
PDB; 6JSH; EM; 5.10 A; C/H/I=1443-1513.
PDB; 6JSI; EM; 4.70 A; C/H/I=1443-1513.
PDB; 6QL5; EM; 2.80 A; A/B/C/D/E/F=1-1887.
PDB; 6QL6; EM; 2.90 A; A/B/C/D/E/F=1-1887.
PDB; 6QL7; X-ray; 4.60 A; A/B/C/D/E/F/a/b/c/d/e/f=1-1887.
PDB; 6QL9; X-ray; 2.82 A; A/B/C/D/E/F=1-1887.
PDB; 6TA1; EM; 3.10 A; A/B/D/F/I/K=1-1887.
PDBsum; 2ML8; -.
PDBsum; 2PFF; -.
PDBsum; 2UV8; -.
PDBsum; 2VKZ; -.
PDBsum; 2WAS; -.
PDBsum; 2WAT; -.
PDBsum; 3HMJ; -.
PDBsum; 6JSH; -.
PDBsum; 6JSI; -.
PDBsum; 6QL5; -.
PDBsum; 6QL6; -.
PDBsum; 6QL7; -.
PDBsum; 6QL9; -.
PDBsum; 6TA1; -.
SMR; P19097; -.
BioGRID; 35931; 387.
ComplexPortal; CPX-1162; Fatty-acyl-CoA synthase.
DIP; DIP-960N; -.
IntAct; P19097; 20.
MINT; P19097; -.
STRING; 4932.YPL231W; -.
iPTMnet; P19097; -.
MaxQB; P19097; -.
PaxDb; P19097; -.
PRIDE; P19097; -.
TopDownProteomics; P19097; -.
EnsemblFungi; YPL231W_mRNA; YPL231W; YPL231W.
GeneID; 855845; -.
KEGG; sce:YPL231W; -.
EuPathDB; FungiDB:YPL231W; -.
SGD; S000006152; FAS2.
GeneTree; ENSGT00940000176444; -.
HOGENOM; CLU_000114_0_0_1; -.
InParanoid; P19097; -.
KO; K00667; -.
OMA; NRWHSES; -.
BioCyc; MetaCyc:YPL231W-MONOMER; -.
BioCyc; YEAST:YPL231W-MONOMER; -.
SABIO-RK; P19097; -.
EvolutionaryTrace; P19097; -.
PRO; PR:P19097; -.
Proteomes; UP000002311; Chromosome XVI.
RNAct; P19097; protein.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005835; C:fatty acid synthase complex; IDA:SGD.
GO; GO:0005739; C:mitochondrion; HDA:SGD.
GO; GO:0102131; F:3-oxo-glutaryl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0102132; F:3-oxo-pimeloyl-[acp] methyl ester reductase activity; IEA:UniProtKB-EC.
GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IDA:SGD.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IMP:SGD.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IMP:SGD.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0071470; P:cellular response to osmotic stress; IDA:SGD.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:SGD.
Gene3D; 3.40.47.10; -; 3.
Gene3D; 3.90.470.20; -; 1.
HAMAP; MF_00101; AcpS; 1.
InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
InterPro; IPR002582; ACPS.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR040899; Fas_alpha_ACP.
InterPro; IPR026025; FAS_alpha_yeast.
InterPro; IPR041550; FASI_helical.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
InterPro; IPR016039; Thiolase-like.
Pfam; PF01648; ACPS; 1.
Pfam; PF18325; Fas_alpha_ACP; 1.
Pfam; PF18314; FAS_I_H; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52151; SSF52151; 1.
SUPFAM; SSF53901; SSF53901; 2.
SUPFAM; SSF56214; SSF56214; 1.
TIGRFAMs; TIGR00556; pantethn_trn; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Magnesium;
Metal-binding; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation.
CHAIN 1..1887
/note="Fatty acid synthase subunit alpha"
/id="PRO_0000180287"
DOMAIN 145..220
/note="Carrier"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
REGION 675..874
/note="Beta-ketoacyl reductase"
REGION 1149..1363
/note="Beta-ketoacyl synthase"
REGION 1772..1774
/note="Acetyl-CoA binding"
REGION 1817..1833
/note="Acetyl-CoA binding"
REGION 1841..1844
/note="Acetyl-CoA binding"
REGION 1871..1873
/note="Acetyl-CoA binding"
ACT_SITE 1305
/note="For beta-ketoacyl synthase activity"
METAL 1772
/note="Magnesium"
METAL 1773
/note="Magnesium; via carbonyl oxygen"
METAL 1774
/note="Magnesium"
METAL 1872
/note="Magnesium"
METAL 1873
/note="Magnesium; via carbonyl oxygen"
BINDING 1798
/note="Acetyl-CoA"
/evidence="ECO:0000269|PubMed:19679086"
BINDING 1808
/note="Acetyl-CoA"
/evidence="ECO:0000269|PubMed:19679086"
MOD_RES 50
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:15665377"
MOD_RES 180
/note="O-(pantetheine 4'-phosphoryl)serine"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
ECO:0000269|PubMed:17431182"
MOD_RES 523
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19779198"
MOD_RES 958
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17330950"
MOD_RES 1440
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:17330950"
CROSSLNK 37
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin)"
/evidence="ECO:0000244|PubMed:22106047"
MUTAGEN 1250
/note="G->S: Cerulenin-resistance."
/evidence="ECO:0000269|PubMed:8041367"
MUTAGEN 1769
/note="V->D: Does not affect oligomerization; when
associated with S-1771 and L-1773 or S-1771; L-1773; S-1879
and E-1881."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1770
/note="G->D: Loss of transferase activity."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1771
/note="V->S: Does not affect oligomerization but lacks
transferase activity; when associated with D-1769 and L-
1773 or D-1769; L-1773; S-1879 and E-1881."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1772
/note="D->S: Loss of transferase activity; when associated
with S-1774."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1773
/note="V->L: Does not affect oligomerization but lacks
transferase activity; when associated with D-1769 and S-
1771 or D-1769; S-1771; S-1879 and E-1881."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1774
/note="E->S: Loss of transferase activity; when associated
with S-1772."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1841
/note="R->A: Loss off transferase activity."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1879
/note="V->S: Does not affect oligomerization but lacks
transferase activity; when associated with D-1769; S-1771;
L-1773 and E-1881."
/evidence="ECO:0000269|PubMed:19679086"
MUTAGEN 1881
/note="V->E: Does not affect oligomerization but lacks
transferase activity; when associated with D-1769; S-1771;
L-1773 and S-1879."
/evidence="ECO:0000269|PubMed:19679086"
CONFLICT 310
/note="G -> GTTGTGG (in Ref. 1; AAA34601)"
/evidence="ECO:0000305"
CONFLICT 594
/note="T -> I (in Ref. 1; AAA34601)"
/evidence="ECO:0000305"
CONFLICT 941..1019
/note="AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVEIQPRANIQLDF
PELKPYKQVKQIAPAELEGLLDLERVI -> CLNCVKSWLKLLKLERQFPSKLLWSIRL
SMAIALMLHMLKSKFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF (in
Ref. 1; AAA34601)"
/evidence="ECO:0000305"
CONFLICT 1036..1041
/note="RWEMEA -> KMGNGS (in Ref. 1; AAA34601)"
/evidence="ECO:0000305"
CONFLICT 1408
/note="A -> S (in Ref. 1; AAA34601)"
/evidence="ECO:0000305"
CONFLICT 1671
/note="N -> T (in Ref. 1; AAA34601)"
/evidence="ECO:0000305"
HELIX 3..20
/evidence="ECO:0000244|PDB:2UV8"
TURN 21..23
/evidence="ECO:0000244|PDB:2UV8"
HELIX 28..37
/evidence="ECO:0000244|PDB:2UV8"
STRAND 42..51
/evidence="ECO:0000244|PDB:2UV8"
HELIX 52..64
/evidence="ECO:0000244|PDB:2UV8"
HELIX 66..71
/evidence="ECO:0000244|PDB:2UV8"
STRAND 77..80
/evidence="ECO:0000244|PDB:2UV8"
TURN 81..83
/evidence="ECO:0000244|PDB:2UV8"
HELIX 85..88
/evidence="ECO:0000244|PDB:2UV8"
HELIX 147..157
/evidence="ECO:0000244|PDB:2UV8"
TURN 158..160
/evidence="ECO:0000244|PDB:2UV8"
TURN 163..165
/evidence="ECO:0000244|PDB:2UV8"
HELIX 172..176
/evidence="ECO:0000244|PDB:2UV8"
HELIX 180..194
/evidence="ECO:0000244|PDB:2UV8"
TURN 201..203
/evidence="ECO:0000244|PDB:2UV8"
HELIX 206..216
/evidence="ECO:0000244|PDB:2UV8"
HELIX 223..236
/evidence="ECO:0000244|PDB:2UV8"
HELIX 243..252
/evidence="ECO:0000244|PDB:2UV8"
TURN 258..260
/evidence="ECO:0000244|PDB:2UV8"
HELIX 261..270
/evidence="ECO:0000244|PDB:2UV8"
STRAND 274..276
/evidence="ECO:0000244|PDB:2ML8"
HELIX 280..298
/evidence="ECO:0000244|PDB:2UV8"
HELIX 329..350
/evidence="ECO:0000244|PDB:2UV8"
HELIX 356..382
/evidence="ECO:0000244|PDB:2UV8"
HELIX 384..389
/evidence="ECO:0000244|PDB:2UV8"
HELIX 396..398
/evidence="ECO:0000244|PDB:2UV8"
STRAND 400..402
/evidence="ECO:0000244|PDB:2UV8"
HELIX 405..421
/evidence="ECO:0000244|PDB:2UV8"
HELIX 430..440
/evidence="ECO:0000244|PDB:2UV8"
HELIX 445..456
/evidence="ECO:0000244|PDB:2UV8"
HELIX 460..462
/evidence="ECO:0000244|PDB:2UV8"
HELIX 464..483
/evidence="ECO:0000244|PDB:2UV8"
STRAND 497..503
/evidence="ECO:0000244|PDB:2UV8"
STRAND 509..515
/evidence="ECO:0000244|PDB:2UV8"
HELIX 522..531
/evidence="ECO:0000244|PDB:2UV8"
TURN 605..607
/evidence="ECO:0000244|PDB:2UV8"
HELIX 609..615
/evidence="ECO:0000244|PDB:2UV8"
HELIX 626..629
/evidence="ECO:0000244|PDB:2UV8"
STRAND 637..643
/evidence="ECO:0000244|PDB:2UV8"
STRAND 649..651
/evidence="ECO:0000244|PDB:2UV8"
HELIX 653..668
/evidence="ECO:0000244|PDB:2UV8"
STRAND 677..682
/evidence="ECO:0000244|PDB:2UV8"
STRAND 685..687
/evidence="ECO:0000244|PDB:2UV8"
HELIX 688..698
/evidence="ECO:0000244|PDB:2UV8"
STRAND 702..709
/evidence="ECO:0000244|PDB:2UV8"
HELIX 712..725
/evidence="ECO:0000244|PDB:2UV8"
STRAND 731..736
/evidence="ECO:0000244|PDB:2UV8"
HELIX 742..753
/evidence="ECO:0000244|PDB:2UV8"
TURN 756..759
/evidence="ECO:0000244|PDB:2UV8"
STRAND 766..770
/evidence="ECO:0000244|PDB:2UV8"
HELIX 781..783
/evidence="ECO:0000244|PDB:2UV8"
HELIX 786..795
/evidence="ECO:0000244|PDB:2UV8"
HELIX 797..811
/evidence="ECO:0000244|PDB:2UV8"
TURN 812..814
/evidence="ECO:0000244|PDB:2UV8"
STRAND 820..826
/evidence="ECO:0000244|PDB:2UV8"
HELIX 839..845
/evidence="ECO:0000244|PDB:2UV8"
HELIX 846..848
/evidence="ECO:0000244|PDB:2UV8"
HELIX 849..855
/evidence="ECO:0000244|PDB:2UV8"
TURN 859..861
/evidence="ECO:0000244|PDB:2UV8"
STRAND 862..869
/evidence="ECO:0000244|PDB:2UV8"
HELIX 885..889
/evidence="ECO:0000244|PDB:2UV8"
HELIX 898..906
/evidence="ECO:0000244|PDB:2UV8"
HELIX 907..909
/evidence="ECO:0000244|PDB:2UV8"
HELIX 911..919
/evidence="ECO:0000244|PDB:2UV8"
STRAND 922..927
/evidence="ECO:0000244|PDB:2UV8"
TURN 930..932
/evidence="ECO:0000244|PDB:2UV8"
STRAND 933..935
/evidence="ECO:0000244|PDB:2UV8"
HELIX 936..968
/evidence="ECO:0000244|PDB:2UV8"
TURN 971..976
/evidence="ECO:0000244|PDB:2UV8"
HELIX 998..1004
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1007..1009
/evidence="ECO:0000244|PDB:2UV8"
TURN 1010..1012
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1015..1017
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1019..1028
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1033..1042
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1047..1056
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1059..1067
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1070..1077
/evidence="ECO:0000244|PDB:2UV8"
TURN 1078..1080
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1086..1088
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1089..1099
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1101..1105
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1108..1111
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1118..1126
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1134..1136
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1138..1148
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1149..1151
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1152..1156
/evidence="ECO:0000244|PDB:2UV8"
TURN 1158..1160
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1163..1167
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1172..1179
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1185..1187
/evidence="ECO:0000244|PDB:2UV8"
TURN 1195..1199
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1202..1207
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1210..1225
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1231..1233
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1234..1237
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1240..1242
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1243..1245
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1248..1251
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1254..1261
/evidence="ECO:0000244|PDB:2UV8"
TURN 1262..1267
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1274..1278
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1282..1290
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1304..1306
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1307..1320
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1325..1333
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1337..1345
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1352..1357
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1362..1364
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1381..1389
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1390..1396
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1402..1410
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1424..1429
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1441..1443
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1445..1474
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1483..1508
/evidence="ECO:0000244|PDB:2UV8"
TURN 1512..1515
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1517..1519
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1521..1527
/evidence="ECO:0000244|PDB:2UV8"
TURN 1528..1530
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1533..1535
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1536..1540
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1547..1564
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1572..1575
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1578..1581
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1585..1587
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1588..1600
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1612..1614
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1616..1620
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1638..1645
/evidence="ECO:0000244|PDB:2UV8"
TURN 1646..1648
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1649..1656
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1659..1662
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1667..1693
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1708..1710
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1711..1716
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1726..1728
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1730..1732
/evidence="ECO:0000244|PDB:2UV8"
TURN 1735..1739
/evidence="ECO:0000244|PDB:2UV8"
HELIX 1742..1745
/evidence="ECO:0000244|PDB:2UV8"
STRAND 1769..1775
/evidence="ECO:0000244|PDB:2WAS"
HELIX 1776..1778
/evidence="ECO:0000244|PDB:2WAS"
HELIX 1784..1790
/evidence="ECO:0000244|PDB:2WAS"
HELIX 1793..1800
/evidence="ECO:0000244|PDB:2WAS"
STRAND 1802..1804
/evidence="ECO:0000244|PDB:2WAS"
HELIX 1805..1823
/evidence="ECO:0000244|PDB:2WAS"
STRAND 1837..1842
/evidence="ECO:0000244|PDB:2WAS"
STRAND 1845..1851
/evidence="ECO:0000244|PDB:2WAS"
HELIX 1853..1860
/evidence="ECO:0000244|PDB:2WAS"
TURN 1861..1863
/evidence="ECO:0000244|PDB:2WAS"
STRAND 1866..1873
/evidence="ECO:0000244|PDB:2WAS"
STRAND 1875..1885
/evidence="ECO:0000244|PDB:2WAS"
SEQUENCE 1887 AA; 206947 MW; 08B872734CF3AEEA CRC64;
MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS PTLAGMAQRT
LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK EEPAKEEAPA PTPAASAPAP
AAAAPAPVAA AAPAAAAAEI ADEPVKASLL LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS
TVQNEILGDL GKEFGTTPEK PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG
FTITVARKYL QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV
DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL KMDLDNGERK
FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR TFDSSWNWAK QSLLSLYFEI
IHGVLKNVDR EVVSEAINIM NRSNDALIKF MEYHISNTDE TKGENYQLVK TLGEQLIENC
KQVLDVDPVY KDVAKPTGPK TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ
PTIEEDLTRV YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD
VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK YDRQLSSLFL
DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG AKVVVTTSRF SKQVTDYYQS
IYAKYGAKGS TLIVVPFNQG SKQDVEALIE FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE
LEHIDSKSEF AHRIMLTNIL RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS
ESKLSLETLF NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE
MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET SEVRKAVSIE
TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ VKQIAPAELE GLLDLERVIV
VTGFAEVGPW GSARTRWEME AFGEFSLEGC VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT
KEPVDDKDVK AKYETSILEH SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET
AEQFKHQHGD KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG MGGVSALRGM
FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT PVGACATSVE SVDIGVETIL
SGKARICIVG GYDDFQEEGS FEFGNMKATS NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ
GAGIQIIMQA DLALKMGVPI YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS
PNLNMKYRKR QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ
LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND KNESATINEM
MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL NSGIIPGNRN ADNVDKILEQ
FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG GQAIVVHPDY LYGAITEDRY NEYVAKVSAR
EKSAYKFFHN GMIYNKLFVS KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS
KDSYINANTI ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS
AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE LHGNAKKAAE
EAGVTDVKVS ISHDDLQAVA VAVSTKK


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Pathways :
WP2199: Seed Development
WP668: Octadecanoid Pathway
WP1566: Citrate cycle (TCA cycle)
WP2347: vitamin B5 (pantothenate) and CoA biosynthesis Pathway
WP211: BMP signaling pathway
WP1403: AMPK signaling
WP1502: Mitochondrial biogenesis
WP2248: anthocyanin biosynthesis
WP1461: Photosynthetic Carbon Reduction
WP210: Cytoplasmic Ribosomal Proteins
WP25: Fatty Acid Beta Oxidation 3
WP1577: amino acid conjugation of benzoic acid
WP401: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP498: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP1307: Fatty Acid Beta Oxidation
WP237: Glucocorticoid & Mineralcorticoid Metabolism
WP1207: Fatty Acid Beta Oxidation
WP209: Fatty Acid Beta Oxidation Meta
WP1621: Arginine and proline metabolism
WP169: Fatty Acid Beta Oxidation 3
WP1226: Mitochondrial LC-Fatty Acid Beta-Oxidation
WP39: Fatty Acid Beta Oxidation 1
WP296: TCA Cycle - biocyc
WP1269: Fatty Acid Beta Oxidation
WP105: Fatty Acid Beta Oxidation 2

Related Genes :
[FAS2 YPL231W P1409] Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
[FAS2 CPAR2_807400] Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl carrier; 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Beta-ketoacyl synthase)]
[atnF ANIA_07880] Fatty acid synthase subunit alpha (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein F) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41)]
[KAS2 FAB1 At1g74960 F25A4.7 F9E10.19] 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic (EC 2.3.1.41) (Beta-ketoacyl-acyl-carrier-protein synthase II) (AtKAS2) (Beta-ketoacyl-ACP synthetase 2) (Protein FATTY ACID BIOSYNTHESIS 1)
[hexA DOTSEDRAFT_66976] Fatty acid synthase alpha subunit hexA (EC 2.3.1.86) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Dothistromin biosynthesis protein hexA)]
[fabG b1093 JW1079] 3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase) (Beta-Ketoacyl-acyl carrier protein reductase) (Beta-ketoacyl-ACP reductase)
[Hsd17b8 H2-Ke6 Hke6] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)
[HSD17B8 FABGL HKE6 RING2 SDR30C1] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Really interesting new gene 2 protein) (Short chain dehydrogenase/reductase family 30C member 1) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)
[atnM ANIA_07873] Fatty acid synthase beta subunit aflB (EC 2.3.1.86) (Aspercryptin biosynthesis cluster protein M) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39); S-acyl fatty acid synthase thioesterase (EC 3.1.2.14)]
[hexB DOTSEDRAFT_181128] Fatty acid synthase beta subunit hexB (EC 2.3.1.86) (S-acyl fatty acid synthase thioesterase) (EC 3.1.2.14) [Includes: 3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59); Enoyl-[acyl-carrier-protein] reductase [NADH] (EC 1.3.1.9); [Acyl-carrier-protein] acetyltransferase (EC 2.3.1.38); [Acyl-carrier-protein] malonyltransferase (EC 2.3.1.39) (Dothistromin biosynthesis protein hexB)]
[fabH b1091 JW1077] 3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase III) (Beta-ketoacyl-ACP synthase III) (KAS III) (EcFabH)
[Hsd17b8] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)
[CBR4 SDR45C1] Carbonyl reductase family member 4 (EC 1.-.-.-) (3-ketoacyl-[acyl-carrier-protein] reductase beta subunit) (KAR beta subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Quinone reductase CBR4) (Short chain dehydrogenase/reductase family 45C member 1)
[hexA] Fatty acid synthase alpha subunit hexA (EC 2.3.1.86) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41) (Dothistromin biosynthesis protein hexA)] (Fragment)
[fabG STM1195] 3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase) (Beta-Ketoacyl-acyl carrier protein reductase) (Beta-ketoacyl-ACP reductase)
[HSD17B8 FABGL HKE6] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)
[HSD17B8] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239)
[At1g24360 F21J9.2 F3I6.30] 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase)
[Cbr4] Carbonyl reductase family member 4 (EC 1.-.-.-) (3-ketoacyl-[acyl-carrier-protein] reductase beta subunit) (KAR beta subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Quinone reductase CBR4)
[ELOVL5 ELOVL2 PRO0530] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Fatty acid elongase 1) (hELO1) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)
[ppsC BQ2027_MB2958] Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsC (Beta-ketoacyl-acyl-carrier-protein synthase I) (EC 2.3.1.41)
[ELOVL7] Elongation of very long chain fatty acids protein 7 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL7) (ELOVL fatty acid elongase 7) (ELOVL FA elongase 7) (Very long chain 3-ketoacyl-CoA synthase 7) (Very long chain 3-oxoacyl-CoA synthase 7)
[HSD17B8] Estradiol 17-beta-dehydrogenase 8 (EC 1.1.1.62) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (EC 1.1.1.-) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239) (Fragment)
[ELOVL4] Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4)
[Elovl4] Elongation of very long chain fatty acids protein 4 (EC 2.3.1.199) (3-keto acyl-CoA synthase Elovl4) (ELOVL fatty acid elongase 4) (ELOVL FA elongase 4) (Very long chain 3-ketoacyl-CoA synthase 4) (Very long chain 3-oxoacyl-CoA synthase 4)
[ELOVL5 QflA-11914] Elongation of very long chain fatty acids protein 5 (EC 2.3.1.199) (3-keto acyl-CoA synthase ELOVL5) (ELOVL fatty acid elongase 5) (ELOVL FA elongase 5) (Very long chain 3-ketoacyl-CoA synthase 5) (Very long chain 3-oxoacyl-CoA synthase 5)
[fabG slr0886] 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase)
[ppsA BQ2027_MB2956] Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsA (Beta-ketoacyl-acyl-carrier-protein synthase I) (EC 2.3.1.41)
[ppsB BQ2027_MB2957] Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsB (Beta-ketoacyl-acyl-carrier-protein synthase I) (EC 2.3.1.41)
[fabH fabH_1 fabH_2 A6581_12495 A6V01_06890 A8C65_09655 A9819_06770 A9R57_10635 A9X72_15425 ACN68_29165 ACN81_09120 ACU57_04235 ACU90_18970 AJ318_01255 AM270_12905 AM464_23490 AMK83_16160 AML07_18230 AML35_01545 APU18_13250 APZ14_01335 ARC77_26460 AU473_14580 AUQ13_23290 AUS26_13725 AW059_19915 AW106_18505 AWB10_15405 AWE53_020510 AWF59_023445 AWG78_002695 AZZ83_000801 B6V57_05465 B9T59_24465 BANRA_01238 BANRA_01626 BANRA_01686 BANRA_04557 BB545_06325 BE963_19735 BEN53_12675 BHF46_12645 BHJ80_09465 BHS81_06845 BHS87_05770 BIQ87_06090 BIZ41_17755 BJJ90_15770 BK248_11900 BK334_17085 BK373_19805 BMA87_09810 BMT49_08385 BN17_09531 BOH76_25745 BON63_21265 BON66_01740 BON69_23345 BON71_18780 BON72_25180 BON75_05130 BON76_26945 BON86_10505 BON91_15375 BON94_01065 BON95_13365 BON96_12855 BTQ04_05110 BTQ06_08090 BUE81_21250 BvCms12BK_01148 BvCms2454_01916 BvCms28BK_04080 BvCms35BK_05129 BvCmsC61A_02382 BvCmsHHP001_05176 BvCmsHHP019_01052 BvCmsHHP056_02914 BvCmsKKP036_01036 BvCmsKSNP073_05165 BvCmsKSNP081_02105 BvCmsKSNP120_02319 BvCmsKSP026_03191 BvCmsKSP058_01396 BvCmsKSP076_00272 BvCmsNSNP036_01505 BvCmsNSP006_01397 BvCmsNSP007_01918 BvCmsOUP014_03076 BvCmsSINP022_02081 BvCmsSIP019_05061 BvCmsSIP044_03787 BW690_19900 BWI89_08590 BWP17_15030 BZL31_08250 C2M16_23610 C2U48_03450 C4K41_10970 C4M78_07510 C5N07_18800 C5P01_13300 C6669_23915 C6B13_08610 C7B02_00830 C7B06_09750 C7B07_08630 C9114_05395 C9141_03435 C9160_03635 C9162_18505 C9201_08320 C9306_08845 C9E25_12645 C9E67_18175 C9Z03_07275 C9Z23_17730 C9Z28_12800 C9Z29_00405 C9Z39_13315 C9Z43_16055 C9Z69_12200 C9Z70_18680 C9Z78_21035 C9Z89_11905 CA593_23030 CDL37_22555 CF006_11860 CG692_05960 CI641_021440 CI694_24350 CIG45_16355 CJU63_06210 CJU64_06165 CMR93_11630 COD30_07215 COD46_12085 CQP61_11630 CR538_15625 CR539_10145 CRD98_10050 CRE06_17995 CRJUMX01_810035 CSB64_06835 CT146_19515 CVH05_05745 CWM24_09700 CWS33_19110 D0X26_19660 D2184_17135 D2185_03660 D3821_20525 D3C88_31960 D3O91_17305 D3P02_01810 D4011_17725 D4023_07705 D4074_16090 D4628_14985 D4636_14965 D4638_10995 D4660_16940 D4718_04210 D4L91_16160 D4M06_16465 D4U85_17815 D4V08_04205 D5H35_12525 D5I97_15245 D6004_10760 D6C36_17140 D6D43_13990 D6T60_02490 D6T98_11690 D6W00_04145 D6X36_18515 D6X63_07045 D6X76_18160 D7K33_14990 D7K63_17605 D7K66_16955 D7Y10_07670 D7Z75_13215 D8Y65_15590 D9610_10405 D9C99_09665 D9D20_13770 D9D44_12170 D9D94_00150 D9E13_03685 D9E19_05135 D9E35_08850 D9E49_23125 D9E73_18200 D9F17_21310 D9F32_18720 D9F87_04065 D9G11_14165 D9G29_04525 D9G69_05350 D9G95_13425 D9H10_18575 D9H36_09275 D9H53_08645 D9H68_09245 D9H94_04295 D9I18_08860 D9I20_14615 D9I87_12745 D9I97_05850 D9J11_10615 D9J44_04910 D9J52_06560 D9J63_11825 D9J78_06070 D9K02_21225 D9K54_27015 D9L89_17030 D9L99_07050 D9S45_08095 D9X77_14405 D9X97_16850 D9Z28_04210 DAH18_03975 DAH26_20105 DAH32_15625 DAH43_20195 DB359_00595 DBQ99_15690 DEN97_07610 DEO04_08940 DEO19_16475 DIV22_29045 DJ487_08090 DJ492_00295 DJ503_02765 DK132_06720 DL251_16745 DL292_12990 DL326_10950 DL455_06820 DL479_07505 DL530_08820 DL545_14895 DL705_14910 DL800_08655 DL979_16830 DLT82_11590 DLU50_11665 DLU67_06830 DLW60_11090 DLW88_12025 DLX38_06620 DLX40_02470 DLY41_15270 DLY44_06835 DM129_01105 DM155_10755 DM267_04265 DM272_07140 DM280_03350 DM820_16310 DM962_14055 DM973_13990 DMI04_15530 DMI53_16425 DMO02_17925 DN627_14115 DN660_15370 DN700_15740 DN703_15615 DN808_13220 DNB37_17090 DNC98_10160 DND79_16250 DNI21_18270 DNJ62_16370 DNK12_14310 DNR35_13685 DNR41_04925 DNX19_06795 DNX30_12130 DOE35_15150 DOM23_05650 DOS18_15615 DOT81_17290 DOU81_15930 DOY22_16740 DOY56_16480 DOY61_09255 DOY67_10855 DP258_00760 DP265_07725 DP277_04960 DQE91_12865 DQF36_07155 DQF57_17370 DQF71_12540 DQF72_08135 DQG35_16760 DQO13_14905 DQP61_14135 DRP48_17500 DRW19_15530 DS143_12075 DS721_15365 DS732_10515 DS966_20430 DT034_08340 DTL43_16260 DTM10_22705 DU333_09965 DVB38_11840 DW236_07020 DWB25_10215 DXT69_19795 DXT73_16715 DXX80_023555 E0I42_05435 E0K84_01825 E2114_05115 E2115_02735 E2119_09445 E2135_09255 E2148_05875 E2855_01361 E2863_01258 E4K55_21795 E4K60_08095 E4K61_12455 E5P22_07810 E5P28_00615 E5P37_16840 E5S46_10850 E5S47_07445 E5S58_15185 E5S61_09395 EA189_03135 EA198_08170 EA200_04540 EA213_13155 EA218_17275 EA222_13485 EA231_20780 EA242_02530 EA245_20690 EA250_00440 EA410_19610 EA429_10945 EA434_20440 EAI42_06925 EAI46_03965 EAI52_09065 EAM59_15180 EAN70_13055 EAN77_15415 EAX79_15010 EB476_13780 EB509_12840 EB510_15075 EB515_17110 EBA46_10695 EBA84_17880 EBJ06_16415 EBM08_08470 EC3234A_26c00620 EC3426_02004 EC382_11775 EC95NR1_05488 ECONIH1_06700 ECs1469 ECTO6_02868 ED225_16350 ED307_13720 ED600_11490 ED607_11495 ED611_17945 ED648_12555 ED903_08105 ED944_18020 EEA45_10380 EEP23_04195 EF082_00095 EF173_18595 EG075_14655 EG599_07955 EG796_11485 EG808_10475 EGC26_12805 EGU87_13450 EH186_02140 EH412_13330 EHD63_15620 EHD79_14950 EHJ36_13255 EHJ66_17650 EHV81_17940 EHV90_11925 EHW09_11875 EHX09_07180 EI021_06780 EI028_16135 EI032_10370 EI041_14260 EIA08_02935 EIZ86_00940 EIZ93_13140 EJ366_13235 EJC75_04295 EKI52_03835 EL75_2654 EL79_2689 EL80_2666 ELT20_13740 ELT23_03310 ELT33_12495 ELT58_01750 ELU85_21660 ELV05_11645 ELV08_10515 ELY05_06780 EPS91_15510 EPS94_06885 EPT01_12400 EPU41_05700 EQ825_00320 ERS085365_03188 ERS085366_02268 ERS085374_00877 ERS085379_02664 ERS085383_03120 ERS085386_02419 ERS085404_02786 ERS085416_00158 ERS139211_01667 ERS150873_02763 ERS150876_03063 EWK56_20070 EXM29_11560 ExPECSC019_00164 ExPECSC038_03492 EXX13_01105 EXX24_14555 EXX71_17100 EXX78_01965 EYD11_13980 EYX82_10585 EYX99_07575 EYY27_12940 EYY78_17880 F1E13_17380 F7F00_15285 F7F11_10310 F7F18_14770 F7F23_14535 F7F26_14505 F7F29_17355 F7G01_16695 F7G03_18550 F9Z74_16180 FE846_17240 FKO60_17360 FQ022_11655 FQ915_17860 FQU83_16780 FQZ46_10940 FRV13_07450 FV293_19575 FV295_00840 FV438_11880 FVB16_04705 FY127_11500 FZ043_09455 GFU40_10910 GFU45_08315 GFU47_13575 GHR40_18545 GII67_14410 GII91_11670 GIY19_00760 GJ11_06565 GJD97_17010 GKE92_05610 GKF28_06055 GKF34_06850 GKF47_06850 GKF74_11540 GKF86_13090 GKF89_00295 GKG08_02415 GKG09_02415 GKG11_02415 GKG12_11070 GKG22_02415 GKG29_02415 GN312_20045 GNZ03_14760 GP654_04200 GP661_08780 GP664_14735 GP666_04140 GP689_02315 GP700_19175 GP720_09235 GP727_12310 GP912_20090 GP935_01660 GP946_02555 GP950_08870 GQA06_08420 GQE22_15805 GQE34_16790 GQE42_09550 GQE58_02510 GQE64_00935 GQE93_16035 GQM13_14330 GQM17_14140 GQN16_04270 GRW80_14820 HmCms184_02396 HmCmsJML079_03032 HmCmsJML146_03648 HmCmsJML204_04503 MJ49_00690 MS6198_12270 MS8345_01074 NCTC10089_03003 NCTC10090_00682 NCTC10766_04446 NCTC10767_05046 NCTC10865_03682 NCTC10974_03414 NCTC11181_00162 NCTC12950_03294 NCTC13127_04068 NCTC13148_05704 NCTC13846_02036 NCTC8179_02876 NCTC8959_00828 NCTC8960_00765 NCTC9001_01010 NCTC9007_01877 NCTC9036_03139 NCTC9045_03548 NCTC9055_04839 NCTC9058_03938 NCTC9062_05293 NCTC9081_03513 NCTC9111_03099 NCTC9117_03834 NCTC9434_03647 NCTC9701_03276 NCTC9703_02305 NCTC9962_06981 NCTC9969_03188 PGD_02204 PU06_15960 RG28_16900 RK56_002865 RX35_02775 SAMEA3472043_03741 SAMEA3472044_03436 SAMEA3472047_01496 SAMEA3472055_02482 SAMEA3472070_03224 SAMEA3472080_03030 SAMEA3472090_04761 SAMEA3472108_02299 SAMEA3472114_01637 SAMEA3484427_03736 SAMEA3484429_03712 SAMEA3485113_04288 SAMEA3752553_01905 SAMEA3752557_01557 SAMEA3752559_02056 SAMEA3752620_04418 SAMEA3753064_00952 SAMEA3753097_03417 SAMEA3753164_01715 SAMEA3753290_02776 SAMEA3753300_01403 SK85_01157 UN86_08245 UN91_19500] 3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase III) (Beta-ketoacyl-ACP synthase III) (KAS III)

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