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Fatty acid synthase alpha subunit aflA (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) (Aflatoxin biosynthesis protein A)]

 AFLA_ASPPU              Reviewed;        1671 AA.
Q8TGA2; A0A0F0HZ47;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-OCT-2017, entry version 101.
RecName: Full=Fatty acid synthase alpha subunit aflA {ECO:0000303|PubMed:16256699};
EC=2.3.1.86 {ECO:0000305|PubMed:16256699};
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000305|PubMed:16256699};
EC=1.1.1.100 {ECO:0000305|PubMed:16256699};
AltName: Full=Beta-ketoacyl reductase {ECO:0000305};
Includes:
RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000305|PubMed:16256699};
EC=2.3.1.41 {ECO:0000305|PubMed:16256699};
AltName: Full=Aflatoxin biosynthesis protein A {ECO:0000303|PubMed:15006741};
Name=aflA {ECO:0000303|PubMed:15006741};
Synonyms=fas-2 {ECO:0000303|PubMed:15094053}, fas-2A,
hexA {ECO:0000303|PubMed:16256699}; ORFNames=P875_00052994;
Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 /
SU-1).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=1403190;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=16256699; DOI=10.1006/bioo.2001.1216;
Hitchman T.S., Schmidt E.W., Trail F., Rarick M.D., Linz J.E.,
Townsend C.A.;
"Hexanoate synthase, a specialized type I fatty acid synthase in
aflatoxin B1 biosynthesis.";
Bioorg. Chem. 29:293-307(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND
NOMENCLATURE.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=15006741; DOI=10.1128/AEM.70.3.1253-1262.2004;
Yu J., Chang P.K., Ehrlich K.C., Cary J.W., Bhatnagar D.,
Cleveland T.E., Payne G.A., Linz J.E., Woloshuk C.P., Bennett J.W.;
"Clustered pathway genes in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 70:1253-1262(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
PubMed=15094053; DOI=10.1016/S0014-5793(04)00327-8;
Yu J., Bhatnagar D., Cleveland T.E.;
"Completed sequence of aflatoxin pathway gene cluster in Aspergillus
parasiticus.";
FEBS Lett. 564:126-130(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1;
Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R.,
Ehrlich K.C., Bhatnagar D., Cleveland T.E., Bennett J.W.,
Nierman W.C.;
"Draft genome sequence of Aspergillus parasiticus SU-1.";
Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION.
PubMed=1339261;
Skory C.D., Chang P.K., Cary J., Linz J.E.;
"Isolation and characterization of a gene from Aspergillus parasiticus
associated with the conversion of versicolorin A to sterigmatocystin
in aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 58:3527-3537(1992).
[6]
FUNCTION.
PubMed=8434913;
Keller N.P., Dischinger H.C. Jr., Bhatnager D., Cleveland T.E.,
Ullah A.H.J.;
"Purification of a 40-kilodalton methyltransferase active in the
aflatoxin biosynthetic pathway.";
Appl. Environ. Microbiol. 59:479-484(1993).
[7]
FUNCTION.
PubMed=8368836;
Yabe K., Matsuyama Y., Ando Y., Nakajima H., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: conversion of
norsolorinic acid to averufin.";
Appl. Environ. Microbiol. 59:2486-2492(1993).
[8]
FUNCTION.
PubMed=8368837;
Yabe K., Hamasaki T.;
"Stereochemistry during aflatoxin biosynthesis: cyclase reaction in
the conversion of versiconal to versicolorin B and racemization of
versiconal hemiacetal acetate.";
Appl. Environ. Microbiol. 59:2493-2500(1993).
[9]
FUNCTION.
PubMed=10543813;
Motomura M., Chihaya N., Shinozawa T., Hamasaki T., Yabe K.;
"Cloning and characterization of the O-methyltransferase I gene (dmtA)
from Aspergillus parasiticus associated with the conversions of
demethylsterigmatocystin to sterigmatocystin and
dihydrodemethylsterigmatocystin to dihydrosterigmatocystin in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 65:4987-4994(1999).
[10]
FUNCTION.
PubMed=10584035;
Zhou R., Linz J.E.;
"Enzymatic function of the nor-1 protein in aflatoxin biosynthesis in
Aspergillus parasiticus.";
Appl. Environ. Microbiol. 65:5639-5641(1999).
[11]
FUNCTION.
PubMed=11055914; DOI=10.1128/AEM.66.11.4715-4719.2000;
Chang P.K., Yu J., Ehrlich K.C., Boue S.M., Montalbano B.G.,
Bhatnagar D., Cleveland T.E.;
"adhA in Aspergillus parasiticus is involved in conversion of 5'-
hydroxyaverantin to averufin.";
Appl. Environ. Microbiol. 66:4715-4719(2000).
[12]
FUNCTION.
PubMed=11996570; DOI=10.1021/ja012185v;
Udwary D.W., Casillas L.K., Townsend C.A.;
"Synthesis of 11-hydroxyl O-methylsterigmatocystin and the role of a
cytochrome P-450 in the final step of aflatoxin biosynthesis.";
J. Am. Chem. Soc. 124:5294-5303(2002).
[13]
FUNCTION.
PubMed=15528514; DOI=10.1128/AEM.70.11.6518-6524.2004;
Ehrlich K.C., Chang P.K., Yu J., Cotty P.J.;
"Aflatoxin biosynthesis cluster gene cypA is required for G aflatoxin
formation.";
Appl. Environ. Microbiol. 70:6518-6524(2004).
[14]
FUNCTION.
PubMed=15932995; DOI=10.1128/AEM.71.6.2999-3006.2005;
Sakuno E., Wen Y., Hatabayashi H., Arai H., Aoki C., Yabe K.,
Nakajima H.;
"Aspergillus parasiticus cyclase catalyzes two dehydration steps in
aflatoxin biosynthesis.";
Appl. Environ. Microbiol. 71:2999-3006(2005).
[15]
FUNCTION.
PubMed=16332900; DOI=10.1128/AEM.71.12.8963-8965.2005;
Ehrlich K.C., Montalbano B., Boue S.M., Bhatnagar D.;
"An aflatoxin biosynthesis cluster gene encodes a novel oxidase
required for conversion of versicolorin a to sterigmatocystin.";
Appl. Environ. Microbiol. 71:8963-8965(2005).
[16]
FUNCTION.
PubMed=15771506; DOI=10.1021/ja0455188;
Henry K.M., Townsend C.A.;
"Ordering the reductive and cytochrome P450 oxidative steps in
demethylsterigmatocystin formation yields general insights into the
biosynthesis of aflatoxin and related fungal metabolites.";
J. Am. Chem. Soc. 127:3724-3733(2005).
[17]
FUNCTION.
PubMed=16461654; DOI=10.1128/AEM.72.2.1096-1101.2006;
Cary J.W., Ehrlich K.C., Bland J.M., Montalbano B.G.;
"The aflatoxin biosynthesis cluster gene, aflX, encodes an
oxidoreductase involved in conversion of versicolorin A to
demethylsterigmatocystin.";
Appl. Environ. Microbiol. 72:1096-1101(2006).
[18]
FUNCTION.
PubMed=18486503; DOI=10.1016/j.fgb.2008.03.003;
Cai J., Zeng H., Shima Y., Hatabayashi H., Nakagawa H., Ito Y.,
Adachi Y., Nakajima H., Yabe K.;
"Involvement of the nadA gene in formation of G-group aflatoxins in
Aspergillus parasiticus.";
Fungal Genet. Biol. 45:1081-1093(2008).
[19]
FUNCTION.
PubMed=18403714; DOI=10.1126/science.1154711;
Crawford J.M., Thomas P.M., Scheerer J.R., Vagstad A.L.,
Kelleher N.L., Townsend C.A.;
"Deconstruction of iterative multidomain polyketide synthase
function.";
Science 320:243-246(2008).
-!- FUNCTION: Fatty acid synthase alpha subunit; part of the gene
cluster that mediates the biosynthesis of aflatoxins, a group of
polyketide-derived furanocoumarins, and part of the most toxic and
carcinogenic compounds among the known mycotoxins
(PubMed:15006741, PubMed:15094053). The four major aflatoxins
produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2
(AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2)
(PubMed:15006741). The first step of the pathway is the conversion
of acetate to norsolorinic acid (NOR) and requires the fatty acid
synthase subunits aflA and aflB, as well as the PKS aflC
(PubMed:15006741). AflC combines a hexanoyl starter unit and 7
malonyl-CoA extender units to synthesize the precursor NOR
(PubMed:18403714). The hexanoyl starter unit is provided to the
acyl-carrier protein (ACP) domain by the fungal fatty acid
synthase aflA/aflB (PubMed:16256699). The second step is the
conversion of NOR to averantin (AVN) and requires the norsolorinic
acid ketoreductase aflD, which catalyzes the dehydration of
norsolorinic acid to form (1'S)-averantin (PubMed:10584035). The
norsolorinic acid reductases aflE and aflF may also play a role in
the conversion of NOR to AVN (PubMed:15006741). The cytochrome
P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to
5'hydroxyaverantin (HAVN) (PubMed:8368836). The next step is
performed by the 5'-hydroxyaverantin dehydrogenase aflH that
transforms HAVN to 5'-oxoaverantin (OAVN) which is further
converted to averufin (AVF) by aflK that plays a dual role in the
pathway, as a 5'-oxoaverantin cyclase that mediates conversion of
5'-oxoaverantin, as well as a versicolorin B synthase in a later
step in the pathway (PubMed:15006741, PubMed:11055914,
PubMed:15932995). The averufin oxidase aflI catalyzes the
conversion of AVF to versiconal hemiacetal acetate (VHA)
(PubMed:15006741). VHA is then the substrate for the versiconal
hemiacetal acetate esterase aflJ to yield versiconal (VAL)
(PubMed:15006741). Versicolorin B synthase aflK then converts VAL
to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin
which is required for DNA-binding, thus giving to aflatoxin its
activity as a mutagen (PubMed:15006741, PubMed:8368837,
PubMed:15932995). Then, the activity of the versicolorin B
desaturase aflL leads to versicolorin A (VERA) (PubMed:15006741,
PubMed:8368837). A branch point starts from VERB since it can also
be converted to dihydrodemethylsterigmatocystin (DMDHST), probably
also by aflL, VERA being a precursor for aflatoxins B1 and G1, and
DMDHST for aflatoxins B2 and G2 (PubMed:15006741). Next, the
versicolorin reductase aflM and the cytochrome P450 monooxygenase
aflN are involved in conversion of VERA to
demethylsterigmatocystin (DMST) (PubMed:15006741, PubMed:1339261,
PubMed:15771506). AflX and aflY seem also involved in this step,
through probable aflX-mediated epoxide ring-opening step following
versicolorin A oxidation and aflY-mediated Baeyer-Villiger
oxidation required for the formation of the xanthone ring
(PubMed:16332900, PubMed:16461654). The methyltransferase aflO
then leads to the modification of DMST to sterigmatocystin (ST),
and of DMDHST to dihydrosterigmatocystin (DHST) (PubMed:10543813).
Both ST and DHST are then substrates of the O-methyltransferase
aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-
methylsterigmatocystin (DHOMST), respectively (PubMed:8434913).
Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to
aflatoxins B2 and G2, via the action of several enzymes including
O-methylsterigmatocystin oxidoreductase aflQ, the cytodhrome P450
monooxygenase aflU, but also the NADH-dependent flavin
oxidoreductase nadA which is specifically required for the
synthesis of AFG1 (PubMed:15006741, PubMed:11996570,
PubMed:15528514, PubMed:18486503). {ECO:0000269|PubMed:10543813,
ECO:0000269|PubMed:10584035, ECO:0000269|PubMed:11055914,
ECO:0000269|PubMed:11996570, ECO:0000269|PubMed:1339261,
ECO:0000269|PubMed:15528514, ECO:0000269|PubMed:15771506,
ECO:0000269|PubMed:15932995, ECO:0000269|PubMed:16256699,
ECO:0000269|PubMed:16332900, ECO:0000269|PubMed:16461654,
ECO:0000269|PubMed:18403714, ECO:0000269|PubMed:18486503,
ECO:0000269|PubMed:8368836, ECO:0000269|PubMed:8368837,
ECO:0000269|PubMed:8434913, ECO:0000305|PubMed:15006741,
ECO:0000305|PubMed:15094053}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-
chain-acyl-CoA + n CoA + n CO(2) + 2n NADP(+).
{ECO:0000305|PubMed:16256699}.
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
[acyl-carrier-protein]. {ECO:0000255|PROSITE-ProRule:PRU10022}.
-!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] +
NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
{ECO:0000305|PubMed:16256699}.
-!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
{ECO:0000269|PubMed:15006741, ECO:0000269|PubMed:15094053,
ECO:0000269|PubMed:16256699}.
-!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional
subunits (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
-!- 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.
-!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit
alpha family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=KJK60794.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF391094; AAL99898.1; -; Genomic_DNA.
EMBL; AY371490; AAS66002.1; -; Genomic_DNA.
EMBL; JZEE01000728; KJK60794.1; ALT_SEQ; Genomic_DNA.
ProteinModelPortal; Q8TGA2; -.
SMR; Q8TGA2; -.
EnsemblFungi; KJK60794; KJK60794; P875_00052994.
UniPathway; UPA00287; -.
Proteomes; UP000033540; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:InterPro.
Gene3D; 3.40.47.10; -; 2.
Gene3D; 3.90.470.20; -; 1.
InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
InterPro; IPR026025; FAS_alpha_yeast.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR013968; PKS_KR.
InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
InterPro; IPR016039; Thiolase-like.
Pfam; PF01648; ACPS; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF08659; KR; 1.
PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
ProDom; PD004282; PPantethiene-prot_Trfase; 1.
SMART; SM00825; PKS_KS; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF53901; SSF53901; 4.
SUPFAM; SSF56214; SSF56214; 1.
TIGRFAMs; TIGR00556; pantethn_trn; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
3: Inferred from homology;
Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism;
Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
Multifunctional enzyme; NADP; Oxidoreductase; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1671 Fatty acid synthase alpha subunit aflA.
/FTId=PRO_0000438336.
DOMAIN 75 153 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258,
ECO:0000305|PubMed:16256699}.
REGION 492 729 Ketoreductase (KR) domain. {ECO:0000255,
ECO:0000305|PubMed:16256699}.
REGION 833 1417 Ketosynthase (KS) domain. {ECO:0000255,
ECO:0000305|PubMed:16256699}.
REGION 1552 1554 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:P19097}.
REGION 1598 1614 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:P19097}.
REGION 1622 1625 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:P19097}.
REGION 1652 1654 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:P19097}.
COMPBIAS 1235 1275 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
ACT_SITE 1113 1113 For beta-ketoacyl synthase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
METAL 1552 1552 Magnesium.
{ECO:0000250|UniProtKB:P19097}.
METAL 1653 1653 Magnesium.
{ECO:0000250|UniProtKB:P19097}.
MOD_RES 113 113 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 1671 AA; 181275 MW; 266034C51A556FFE CRC64;
MVIQGKRLAA SSIQLLASSL DAKKLCYEYD ERQAPGVTQI TEEAPTEQPP LSTPPSLPQT
PNISPISASK IVIDDVALSR VQIVQALVAR KLKTAIAQLP TSKSIKELSG GRSSLQNELV
GDIHNEFSSI PDAPEQILLR DFGDANPTVQ LGKTSSAAVA KLISSKMPSD FNANAIRAHL
ANKWGLGPLR QTAVLLYAIA SEPPSRLASS SAAEEYWDNV SSMYAESCGI TLRPRQDTMN
EDAMASSAID PAVVAEFSKG HRRLGVQQFQ ALAEYLQIDL SGSQASQSDA LVAELQQKVD
LWTAEMTPEF LAGISPMLDV KKSRRYGSWW NMARQDVLAF YRRPSYSEFV DDALAFKVFL
NRLCNRADEA LLNMVRSLSC DAYFKQGSLP GYHAASRLLE QAITSTVADC PKARLILPAV
GPHTTITKDG TIEYAEAPRQ GVSGPTAYIQ SLRQGASFIG LKSADVDTQS NLTDALLDAM
CLALHNGISF VGKTFLVTGA GQGSIGAGVV RLLLEGGARV LVTTSREPAT TSRYFQQMYD
NHGAKFSELR VVPCNLASAQ DCEGLIRHVY DPRGLNWDLD AILPFAAASD YSTEMHDIRG
QSELGHRLML VNVFRVLGHI VHCKRDAGVD CHPTQVLLPL SPNHGIFGGD GMYPESKLAL
ESLFHRIRSE SWSDQLSICG VRIGWTRSTG LMTAHDIIAE TVEEHGIRTF SVAEMALNIA
MLLTPDFVAH CEDGPLDADF TGSLGTLGSI PGFLAQLHQK VQLAAEVIRA VQAEDEHERF
LSPGTKPTLQ APVAPMHPRS SLRVGYPRLP DYEQEIRPLS PRLERLQDPA NAVVVVGYSE
LGPWGSARLR WEIESQGQWT SAGYVELAWL MNLIRHVNDE SYVGWVDTQT GKPVRDGEIQ
ALYGDHIDNH TGIRPIQSTS YNPERMEVLQ EVAVEEDLPE FEVSQLTADA MRLRHGANVS
IRPSGNPDAC HVKLKRGAVI LVPKTVPFVW GSCAGELPKG WTPAKYGIPE NLIHQVDPVT
LYTICCVAEA FYSAGITHPL EVFRHIHLSE LGNFIGSSMG GPTKTRQLYR DVYFDHEIPS
DVLQDTYLNT PAAWVNMLLL GCTGPIKTPV GACATGVESI DSGYESIMAG KTKMCLVGGY
DDLQEEASYG FAQLKATVNV EEEIACGRQP SEMSRPMAES RAGFVEAHGC GVQLLCRGDI
ALQMGLPIYA VIASSAMAAD KIGSSVPAPG QGILSFSRER ARSSMISVTS RPSSRSSTSS
EVSDKSSLTS ITSISNPAPR AQRARSTTDM APLRAALATW GLTIDDLDVA SLHGTSTRGN
DLNEPEVIET QMRHLGRTPG RPLWAICQKS VTGHPKAPAA AWMLNGCLQV LDSGLVPGNR
NLDTLDEALR SASHLCFPTR TVQLREVKAF LLTSFGFGQK GGQVVGVAPK YFFATLPRPE
VEGYYRKVRV RTEAGDRAYA AAVMSQAVVK IQTQNPYDEP DAPRIFLDPL ARISQDPSTG
QYRFRSDATP ALDDDALPPP GEPTELVKGI SSAWIEEKVR PHMSPGGTVG VDLVPLASFD
AYKNAIFVER NYTVRERDWA EKSADVRAAY ASRWCAKEAV FKCLQTHSQG AGAAMKEIEI
EHGGNGAPKV KLRGAAQTAA RQRGLEGVQL SISYGDDAVI AVALGLMSGA S


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EIAAB11118 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,FABGL,HKE6,HSD17B8,Ke-6,Pig,Protein Ke6,Sus scrofa,Testosterone 17-bet
EIAAB11119 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,FABGL,HKE6,Homo sapiens,HSD17B8,Human,Ke-6,Protein Ke6,Really interest
OXSM_BOVIN ELISA Kit FOR 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial; organism: Bovine; gene name: OXSM 96T
EIAAB11117 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Estradiol 17-beta-dehydrogenase 8,Hsd17b8,Rat,Rattus norvegicus,Testosterone 17-beta-dehydrogenase 8
EIAAB11120 17-beta-HSD 8,17-beta-hydroxysteroid dehydrogenase 8,3-oxoacyl-[acyl-carrier-protein] reductase,Canis familiaris,Canis lupus familiaris,Dog,Estradiol 17-beta-dehydrogenase 8,HSD17B8,Testosterone 17-be
EIAAB12849 3-keto acyl-CoA synthase ELOVL6,Elongation of very long chain fatty acids protein 6,ELOVL6,FACE,Fatty acid elongase 2,Fatty acyl-CoA elongase,hELO2,Homo sapiens,Human,LCE,Long-chain fatty-acyl elongas
EIAAB12846 3-keto acyl-CoA synthase Elovl6,Elongation of very long chain fatty acids protein 6,Elovl6,Face,Fatty acid elongase 2,Fatty acyl-CoA elongase,Lce,Long-chain fatty-acyl elongase,Rat,Rattus norvegicus,r
abx109426 Polyclonal Rabbit Enoyl-[acyl-carrier-protein] reductase [NADH] Antibody 100 μg
abx109170 Polyclonal Rabbit Enoyl-[acyl-carrier-protein] reductase [NADH] Antibody (HRP) 100 μg
EIAAB12848 3-keto acyl-CoA synthase Elovl6,Elongation of very long chain fatty acids protein 6,Elovl6,Face,Fatty acyl-CoA elongase,Lce,Long chain fatty acid elongase,Masr,Mouse,Mus musculus,Myelin-associated SUR


 

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