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Acetyl-CoA carboxylase 1 (AtACC1) (EC 6.4.1.2) (Protein EMBRYO DEFECTIVE 22) (Protein GURKE) (Protein PASTICCINO 3) [Includes: Biotin carboxylase (EC 6.3.4.14)]

 ACC1_ARATH              Reviewed;        2254 AA.
Q38970; Q0WNF3; Q38971; Q9C8G1; Q9SKV1;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 140.
RecName: Full=Acetyl-CoA carboxylase 1;
Short=AtACC1;
EC=6.4.1.2 {ECO:0000269|PubMed:9008389};
AltName: Full=Protein EMBRYO DEFECTIVE 22;
AltName: Full=Protein GURKE;
AltName: Full=Protein PASTICCINO 3;
Includes:
RecName: Full=Biotin carboxylase;
EC=6.3.4.14;
Name=ACC1; Synonyms=EMB22, GK, PAS3; OrderedLocusNames=At1g36160;
ORFNames=F15C21.1;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=7915036; DOI=10.1104/pp.105.2.611;
Roesler K.R., Shorrosh B.S., Ohlrogge J.B.;
"Structure and expression of an Arabidopsis acetyl-coenzyme A
carboxylase gene.";
Plant Physiol. 105:611-617(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=7551584; DOI=10.1093/oxfordjournals.pcp.a078822;
Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J.,
Ichikawa N.;
"Genomic organization of 251 kDa acetyl-CoA carboxylase genes in
Arabidopsis: tandem gene duplication has made two differentially
expressed isozymes.";
Plant Cell Physiol. 36:779-787(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1246-2254.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
DISRUPTION PHENOTYPE.
PubMed=9011083; DOI=10.1046/j.1365-313X.1996.10061005.x;
Torres-Ruiz R.A., Lohner A., Juergens G.;
"The GURKE gene is required for normal organization of the apical
region in the Arabidopsis embryo.";
Plant J. 10:1005-1016(1996).
[7]
FUNCTION, AND CATALYTIC ACTIVITY AS ACETYL-COA CARBOXYLASE.
PubMed=9008389; DOI=10.1104/pp.113.1.75;
Roesler K., Shintani D., Savage L., Boddupalli S., Ohlrogge J.;
"Targeting of the Arabidopsis homomeric acetyl-coenzyme A carboxylase
to plastids of rapeseeds.";
Plant Physiol. 113:75-81(1997).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=9449673;
Faure J.-D., Vittorioso P., Santoni V., Fraisier V., Prinsen E.,
Barlier I., Van Onckelen H., Caboche M., Bellini C.;
"The PASTICCINO genes of Arabidopsis thaliana are involved in the
control of cell division and differentiation.";
Development 125:909-918(1998).
[9]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12376641; DOI=10.1104/pp.008110;
Fatland B.L., Ke J., Anderson M.D., Mentzen W.I., Cui L.W.,
Allred C.C., Johnston J.L., Nikolau B.J., Wurtele E.S.;
"Molecular characterization of a heteromeric ATP-citrate lyase that
generates cytosolic acetyl-coenzyme A in Arabidopsis.";
Plant Physiol. 130:740-756(2002).
[10]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Wassilewskija;
PubMed=12943542; DOI=10.1046/j.1365-313X.2003.016010.x;
Baud S., Guyon V., Kronenberger J., Wuilleme S., Miquel M.,
Caboche M., Lepiniec L., Rochat C.;
"Multifunctional acetyl-CoA carboxylase 1 is essential for very long
chain fatty acid elongation and embryo development in Arabidopsis.";
Plant J. 33:75-86(2003).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-1588 AND
GLY-1787.
STRAIN=cv. Wassilewskija;
PubMed=15088065; DOI=10.1038/sj.embor.7400124;
Baud S., Bellec Y., Miquel M., Bellini C., Caboche M., Lepiniec L.,
Faure J.D., Rochat C.;
"gurke and pasticcino3 mutants affected in embryo development are
impaired in acetyl-CoA carboxylase.";
EMBO Rep. 5:515-520(2004).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15509834; DOI=10.1093/pcp/pch148;
Kajiwara T., Furutani M., Hibara K., Tasaka M.;
"The GURKE gene encoding an acetyl-CoA carboxylase is required for
partitioning the embryo apex into three subregions in Arabidopsis.";
Plant Cell Physiol. 45:1122-1128(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1031 AND SER-1192, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[14]
FUNCTION.
PubMed=20145257; DOI=10.1105/tpc.109.071209;
Roudier F., Gissot L., Beaudoin F., Haslam R., Michaelson L.,
Marion J., Molino D., Lima A., Bach L., Morin H., Tellier F.,
Palauqui J.C., Bellec Y., Renne C., Miquel M., Dacosta M., Vignard J.,
Rochat C., Markham J.E., Moreau P., Napier J., Faure J.D.;
"Very-long-chain fatty acids are involved in polar auxin transport and
developmental patterning in Arabidopsis.";
Plant Cell 22:364-375(2010).
[15]
REVIEW, AND NOMENCLATURE.
PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y.,
Yamazaki M., Tohge T., Fernie A.R.;
"The flavonoid biosynthetic pathway in Arabidopsis: Structural and
genetic diversity.";
Plant Physiol. Biochem. 72:21-34(2013).
-!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation
of acetyl-CoA, forming malonyl-CoA, which is used in the plastid
for fatty acid synthesis and in the cytosol in various
biosynthetic pathways including fatty acid elongation. Required
for very long chain fatty acids elongation. Necessary for embryo
and plant development. Plays a central function in embryo
morphogenesis, especially in apical meristem development. Involved
in cell proliferation and tissue patterning. May act as a
repressor of cytokinin response. {ECO:0000269|PubMed:12943542,
ECO:0000269|PubMed:15088065, ECO:0000269|PubMed:15509834,
ECO:0000269|PubMed:20145257, ECO:0000269|PubMed:9008389,
ECO:0000269|PubMed:9449673}.
-!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
+ malonyl-CoA. {ECO:0000269|PubMed:9008389}.
-!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] +
HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-
protein]. {ECO:0000250|UniProtKB:O04983}.
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000250};
-!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
from acetyl-CoA: step 1/1.
-!- SUBUNIT: Homodimer. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in roots, trichomes, epidermal leaf
cells, siliques, petals, anthers, and seeds.
{ECO:0000269|PubMed:12376641, ECO:0000269|PubMed:12943542,
ECO:0000269|PubMed:7551584, ECO:0000269|PubMed:7915036}.
-!- DEVELOPMENTAL STAGE: Expressed in flower buds at stage 6 of
development in tapetal cells and at stage 10 in the epidermal
cells of growing petals and ovaries. In young siliques, expressed
transiently in the inner integument of the ovules just prior to
testal deposition. {ECO:0000269|PubMed:12376641}.
-!- DISRUPTION PHENOTYPE: Embryo lethal with an arrest in development
at the late globular stage in acc1-1 and acc1-2 null allele
mutants. In the leaky pas3 and gk alleles, defect in embryo
development, very short and thick hypocotyl and misshaped
cotyledons that do not expand. Abnormal root development, abnormal
fused leaves and compact rosettes with multiple shoots.
Uncoordinated cell divisions in the apical region. Reduced levels
of very long chain fatty acids in seeds.
{ECO:0000269|PubMed:12943542, ECO:0000269|PubMed:15088065,
ECO:0000269|PubMed:15509834, ECO:0000269|PubMed:9011083,
ECO:0000269|PubMed:9449673}.
-!- MISCELLANEOUS: The acc1-1 and pas3-1 mutants can be partially
complemented by exogenous supply of malonate.
-!- SEQUENCE CAUTION:
Sequence=AAF18638.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAG51250.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; L27074; AAC41645.1; -; Genomic_DNA.
EMBL; D34630; BAA07012.1; -; mRNA.
EMBL; AF062308; AAG40563.1; -; Genomic_DNA.
EMBL; AC006228; AAF18638.2; ALT_SEQ; Genomic_DNA.
EMBL; AC025781; AAG51250.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE31849.1; -; Genomic_DNA.
EMBL; CP002684; AEE31850.1; -; Genomic_DNA.
EMBL; AK229488; BAF01346.1; -; mRNA.
PIR; D86483; D86483.
RefSeq; NP_001185143.1; NM_001198214.2.
RefSeq; NP_174849.2; NM_103313.4.
UniGene; At.39402; -.
ProteinModelPortal; Q38970; -.
SMR; Q38970; -.
BioGrid; 25753; 4.
IntAct; Q38970; 1.
STRING; 3702.AT1G36160.1; -.
iPTMnet; Q38970; -.
PaxDb; Q38970; -.
PRIDE; Q38970; -.
EnsemblPlants; AT1G36160.1; AT1G36160.1; AT1G36160.
EnsemblPlants; AT1G36160.2; AT1G36160.2; AT1G36160.
GeneID; 840521; -.
Gramene; AT1G36160.1; AT1G36160.1; AT1G36160.
Gramene; AT1G36160.2; AT1G36160.2; AT1G36160.
KEGG; ath:AT1G36160; -.
Araport; AT1G36160; -.
TAIR; locus:2034310; AT1G36160.
eggNOG; KOG0368; Eukaryota.
eggNOG; COG0439; LUCA.
eggNOG; COG0511; LUCA.
eggNOG; COG4799; LUCA.
HOGENOM; HOG000214115; -.
InParanoid; Q38970; -.
KO; K11262; -.
OMA; QAHYDKC; -.
OrthoDB; EOG0936001E; -.
PhylomeDB; Q38970; -.
BioCyc; ARA:AT1G36160-MONOMER; -.
BRENDA; 6.4.1.2; 399.
Reactome; R-ATH-163765; ChREBP activates metabolic gene expression.
Reactome; R-ATH-196780; Biotin transport and metabolism.
Reactome; R-ATH-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-ATH-75105; Fatty acyl-CoA biosynthesis.
UniPathway; UPA00655; UER00711.
PRO; PR:Q38970; -.
Proteomes; UP000006548; Chromosome 1.
Genevisible; Q38970; AT.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0030497; P:fatty acid elongation; IMP:TAIR.
GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
GO; GO:0010072; P:primary shoot apical meristem specification; IMP:TAIR.
GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
GO; GO:0048364; P:root development; IMP:TAIR.
GO; GO:0048367; P:shoot system development; IMP:TAIR.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR034733; AcCoA_carboxyl.
InterPro; IPR013537; AcCoA_COase_cen.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR005481; BC-like_N.
InterPro; IPR001882; Biotin_BS.
InterPro; IPR011764; Biotin_carboxylation_dom.
InterPro; IPR005482; Biotin_COase_C.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR011763; COA_CT_C.
InterPro; IPR011762; COA_CT_N.
InterPro; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF08326; ACC_central; 1.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF01039; Carboxyl_trans; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52096; SSF52096; 2.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS50989; COA_CT_CTER; 1.
PROSITE; PS50980; COA_CT_NTER; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
Allosteric enzyme; ATP-binding; Biotin; Complete proteome; Cytoplasm;
Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Reference proteome.
CHAIN 1 2254 Acetyl-CoA carboxylase 1.
/FTId=PRO_0000412211.
DOMAIN 36 543 Biotin carboxylation.
DOMAIN 189 381 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 670 744 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 1492 1831 CoA carboxyltransferase N-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01136}.
DOMAIN 1835 2150 CoA carboxyltransferase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU01137}.
NP_BIND 215 272 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
REGION 1492 2150 Carboxyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU01138}.
ACT_SITE 356 356 {ECO:0000250}.
METAL 338 338 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 352 352 Magnesium or manganese 1.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 352 352 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
METAL 354 354 Magnesium or manganese 2.
{ECO:0000255|PROSITE-ProRule:PRU00409}.
BINDING 1740 1740 Coenzyme A. {ECO:0000250}.
BINDING 2041 2041 Coenzyme A. {ECO:0000250}.
BINDING 2043 2043 Coenzyme A. {ECO:0000250}.
MOD_RES 711 711 N6-biotinyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
MOD_RES 1031 1031 Phosphothreonine.
{ECO:0000244|PubMed:19376835}.
MOD_RES 1192 1192 Phosphoserine.
{ECO:0000244|PubMed:19376835}.
MUTAGEN 1588 1588 E->K: In pas3-1; developmental phenotype
and reduced levels of very long chain
fatty acids in seeds.
{ECO:0000269|PubMed:15088065}.
MUTAGEN 1787 1787 G->S: In pas3-2; developmental phenotype
and reduced levels of very long chain
fatty acids in seeds.
{ECO:0000269|PubMed:15088065}.
CONFLICT 337 337 V -> I (in Ref. 1; AAC41645 and 2;
AAG40563). {ECO:0000305}.
CONFLICT 1378 1379 EQ -> DE (in Ref. 1; AAC41645 and 2;
AAG40563). {ECO:0000305}.
SEQUENCE 2254 AA; 251382 MW; F00A5AE316CC5E87 CRC64;
MAGSVNGNHS AVGPGINYET VSQVDEFCKA LRGKRPIHSI LIANNGMAAV KFIRSVRTWA
YETFGTEKAI LLVGMATPED MRINAEHIRI ADQFVEVPGG TNNNNYANVQ LIVEMAEVTR
VDAVWPGWGH ASENPELPDA LDAKGIIFLG PPASSMAALG DKIGSSLIAQ AADVPTLPWS
GSHVKIPPNS NLVTIPEEIY RQACVYTTEE AIASCQVVGY PAMIKASWGG GGKGIRKVHN
DDEVRALFKQ VQGEVPGSPI FIMKVASQSR HLEVQLLCDK HGNVSALHSR DCSVQRRHQK
IIEEGPITVA PPETVKKLEQ AARRLAKSVN YVGAATVEYL YSMDTGEYYF LELNPRLQVE
HPVTEWIAEI NLPAAQVAVG MGIPLWQIPE IRRFYGIEHG GGYDSWRKTS VVAFPFDFDK
AQSIRPKGHC VAVRVTSEDP DDGFKPTSGR VQELSFKSKP NVWAYFSVKS GGGIHEFSDS
QFGHVFAFGE SRALAIANMV LGLKEIQIRG EIRTNVDYTI DLLHASDYRD NKIHTGWLDS
RIAMRVRAER PPWYLSVVGG ALYKASATSA AVVSDYVGYL EKGQIPPKHI SLVHSQVSLN
IEGSKYTIDV VRGGSGTYRL RMNKSEVVAE IHTLRDGGLL MQLDGKSHVI YAEEEAAGTR
LLIDGRTCLL QNDHDPSKLM AETPCKLMRY LISDNSNIDA DTPYAEVEVM KMCMPLLSPA
SGVIHFKMSE GQAMQAGELI ANLDLDDPSA VRKAEPFHGS FPRLGLPTAI SGRVHQRCAA
TLNAARMILA GYEHKVDEVV QDLLNCLDSP ELPFLQWQEC FAVLATRLPK NLRNMLESKY
REFESISRNS LTTDFPAKLL KGILEAHLSS CDEKERGALE RLIEPLMSLA KSYEGGRESH
ARVIVHSLFE EYLSVEELFN DNMLADVIER MRQLYKKDLL KIVDIVLSHQ GIKNKNKLVL
RLMEQLVYPN PAAYRDKLIR FSTLNHTNYS ELALKASQLL EQTKLSELRS NIARSLSELE
MFTEDGENMD TPKRKSAINE RIEDLVSASL AVEDALVGLF DHSDHTLQRR VVETYIRRLY
QPYVVKDSVR MQWHRSGLLA SWEFLEEHME RKNIGLDDPD TSEKGLVEKR SKRKWGAMVI
IKSLQFLPSI ISAALRETKH NDYETAGAPL SGNMMHIAIV GINNQMSLLQ DSGDEDQAQE
RVNKLAKILK EEEVSSSLCS AGVGVISCII QRDEGRTPMR HSFHWSLEKQ YYVEEPLLRH
LEPPLSIYLE LDKLKGYSNI QYTPSRDRQW HLYTVTDKPV PIKRMFLRSL VRQATMNDGF
ILQQGQDKQL SQTLISMAFT SKCVLRSLMD AMEELELNAH NAAMKPDHAH MFLCILREQQ
IDDLVPFPRR VEVNAEDEET TVEMILEEAA REIHRSVGVR MHRLGVCEWE VRLWLVSSGL
ACGAWRVVVA NVTGRTCTVH IYREVETPGR NSLIYHSITK KGPLHETPIS DQYKPLGYLD
RQRLAARRSN TTYCYDFPLA FGTALELLWA SQHPGVKKPY KDTLINVKEL VFSKPEGSSG
TSLDLVERPP GLNDFGMVAW CLDMSTPEFP MGRKLLVIAN DVTFKAGSFG PREDAFFLAV
TELACAKKLP LIYLAANSGA RLGVAEEVKA CFKVGWSDEI SPENGFQYIY LSPEDHERIG
SSVIAHEVKL SSGETRWVID TIVGKEDGIG VENLTGSGAI AGAYSKAYNE TFTLTFVSGR
TVGIGAYLAR LGMRCIQRLD QPIILTGFST LNKLLGREVY SSHMQLGGPK IMGTNGVVHL
TVSDDLEGVS AILNWLSYIP AYVGGPLPVL APLDPPERIV EYVPENSCDP RAAIAGVKDN
TGKWLGGIFD KNSFIETLEG WARTVVTGRA KLGGIPVGVV AVETQTVMQI IPADPGQLDS
HERVVPQAGQ VWFPDSAAKT AQALMDFNRE ELPLFILANW RGFSGGQRDL FEGILQAGST
IVENLRTYRQ PVFVYIPMMG ELRGGAWVVV DSQINSDYVE MYADETARGN VLEPEGTIEI
KFRTKELLEC MGRLDQKLIS LKAKLQDAKQ SEAYANIELL QQQIKAREKQ LLPVYIQIAT
KFAELHDTSM RMAAKGVIKS VVEWSGSRSF FYKKLNRRIA ESSLVKNVRE ASGDNLAYKS
SMRLIQDWFC NSDIAKGKEE AWTDDQVFFT WKDNVSNYEL KLSELRAQKL LNQLAEIGNS
SDLQALPQGL ANLLNKVEPS KREELVAAIR KVLG


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Catalog number Product name Quantity
E1284m ELISA Acac,Acaca,ACC1,ACC-alpha,Acetyl-CoA carboxylase 1,Acetyl-CoA carboxylase 265,Gm738,Mouse,Mus musculus 96T
E1284m ELISA kit Acac,Acaca,ACC1,ACC-alpha,Acetyl-CoA carboxylase 1,Acetyl-CoA carboxylase 265,Gm738,Mouse,Mus musculus 96T
U1284m CLIA Acac,Acaca,ACC1,ACC-alpha,Acetyl-CoA carboxylase 1,Acetyl-CoA carboxylase 265,Gm738,Mouse,Mus musculus 96T
ACC21-C Recombinant Human Acetyl-CoA Carboxylase-2 (ACC-2) protein control for Western 100 ul
ACC11-C Recombinant Human Acetyl-CoA Carboxylase-1 (ACC-1) protein control for Western 100 ul
EIAAB45818 Gamma-glutamyl carboxylase,GC,GGCX,Homo sapiens,Human,Peptidyl-glutamate 4-carboxylase,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
A0110 Acetyl-CoA Carboxylase Primary Antibody, ACACA, Species: Human Recombinant Protein Source: Rabbit Polyclonal 50ug
EIAAB45817 Bos taurus,Bovine,Gamma-glutamyl carboxylase,GC,GGCX,Peptidyl-glutamate 4-carboxylase,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
EIAAB45820 Gamma-glutamyl carboxylase,Ggcx,Mouse,Mus musculus,Peptidyl-glutamate 4-carboxylase,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
EIAAB45819 Gamma-glutamyl carboxylase,Ggcx,Peptidyl-glutamate 4-carboxylase,Rat,Rattus norvegicus,Vitamin K gamma glutamyl carboxylase,Vitamin K-dependent gamma-carboxylase
bs-2745R-Biotin Rabbit Anti-Acetyl CoA Carboxylase Polyclonal Antibody, Biotin Conjugated 100ul
bs-2745R-Biotin Rabbit Anti-Acetyl CoA Carboxylase Polyclonal Antibody, Biotin Conjugated 100ug
ACC21-C Recombinant Human Acetyl-CoA Carboxylase-2 (ACC-2) protein control for Western Species Reactivity: Human 100 ul Product tipe: Werstern control
ACC11-C Recombinant Human Acetyl-CoA Carboxylase-1 (ACC-1) protein control for Western Species Reactivity: Human 100 ul Product tipe: Werstern control
bs-2745R-Biotin Rabbit Anti-Acetyl CoA Carboxylase Polyclonal Antibody, Biotin conjugated, Isotype: IgG 100ug Lyophilized
bs-3039R-Biotin Rabbit Anti-Phospho-Acetyl CoA Carboxylase(Ser79) Polyclonal Antibody, Biotin Conjugated 100ul
bs-3036R-Biotin Rabbit Anti-Phospho-Acetyl CoA Carboxylase(Ser79) Polyclonal Antibody, Biotin Conjugated 100ug
bs-3036R-Biotin Rabbit Anti-Phospho-Acetyl CoA Carboxylase(Ser79) Polyclonal Antibody, Biotin conjugated, Isotype: IgG 100ug Lyophilized
bs-12955R-Biotin Rabbit Anti-phospho-Acetyl Coenzyme A Carboxylase alpha (Ser12 Polyclonal Antibody, Biotin Conjugated 100ul
bs-12952R-Biotin Rabbit Anti-phospho-Acetyl Coenzyme A Carboxylase beta (Ser22 Polyclonal Antibody, Biotin Conjugated 100ul
bs-12954R-Biotin Rabbit Anti-phospho-Acetyl Coenzyme A Carboxylase alpha (Ser80 Polyclonal Antibody, Biotin Conjugated 100ul
bs-3036R-Biotin Rabbit Anti-Phospho-Acetyl Coenzyme A carboxylase alpha (Ser78 Polyclonal Antibody, Biotin Conjugated 100ul
EIAAB33256 Homo sapiens,Human,PC,PCB,Pyruvate carboxylase, mitochondrial,Pyruvic carboxylase
EIAAB33259 Mouse,Mus musculus,Pc,PCB,Pcx,Pyruvate carboxylase, mitochondrial,Pyruvic carboxylase
EIAAB33258 Bos taurus,Bovine,PC,PCB,Pyruvate carboxylase, mitochondrial,Pyruvic carboxylase


 

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