GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha)

 MCCA_HUMAN              Reviewed;         725 AA.
Q96RQ3; Q59ES4; Q9H959; Q9NS97;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 3.
13-FEB-2019, entry version 196.
RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial;
Short=MCCase subunit alpha;
EC=6.4.1.4;
AltName: Full=3-methylcrotonyl-CoA carboxylase 1;
AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit;
AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha;
Flags: Precursor;
Name=MCCC1; Synonyms=MCCA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INVOLVEMENT IN MCC1D, AND VARIANTS MCC1D
ARG-325 AND SER-385.
PubMed=11170888; DOI=10.1086/318202;
Gallardo M.E., Desviat L.R., Rodriguez J.M., Esparza-Gordillo J.,
Perez-Cerda C., Perez B., Rodriguez-Pombo P., Criado O., Sanz R.,
Morton D.H., Gibson K.M., Le T.P., Ribes A., Rodriguez de Cordoba S.,
Ugarte M., Penalva M.A.;
"The molecular basis of 3-methylcrotonylglycinuria, a disorder of
leucine catabolism.";
Am. J. Hum. Genet. 68:334-346(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11401427; DOI=10.1006/geno.2000.6366;
Obata K., Fukuda T., Morishita R., Abe S., Asakawa S., Yamaguchi S.,
Yoshino M., Ihara K., Murayama K., Shigemoto K., Shimizu N., Kondo I.;
"Human biotin-containing subunit of 3-methylcrotonyl-CoA carboxylase
gene (MCCA): cDNA sequence, genomic organization, localization to
chromosomal band 3q27, and expression.";
Genomics 72:145-152(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT MCC1D PHE-535, AND VARIANT
PRO-464.
PubMed=11406611; DOI=10.1093/hmg/10.12.1299;
Holzinger A., Roeschinger W., Lagler F., Mayerhofer P.U., Lichtner P.,
Kattenfeld T., Thuy L.P., Nyhan W.L., Koch H.G., Muntau A.C.,
Roscher A.A.;
"Cloning of the human MCCA and MCCB genes and mutations therein reveal
the molecular cause of 3-methylcrotonyl-CoA: carboxylase deficiency.";
Hum. Mol. Genet. 10:1299-1306(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MCC1D VAL-289; SER-385; PRO-437
AND HIS-532, AND VARIANT PRO-464.
PubMed=11181649; DOI=10.1172/JCI11948;
Baumgartner M.R., Almashanu S., Suormala T., Obie C., Cole R.N.,
Packman S., Baumgartner E.R., Valle D.;
"The molecular basis of human 3-methylcrotonyl-CoA carboxylase
deficiency.";
J. Clin. Invest. 107:495-504(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-464.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MCC1D TRP-232, AND
VARIANT PRO-464.
TISSUE=Aorta;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-464.
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 42-47, AND SUBCELLULAR LOCATION.
TISSUE=Kidney;
PubMed=16023992; DOI=10.1016/j.bbrc.2005.06.190;
Stadler S.C., Polanetz R., Meier S., Mayerhofer P.U., Herrmann J.M.,
Anslinger K., Roscher A.A., Roschinger W., Holzinger A.;
"Mitochondrial targeting signals and mature peptides of 3-
methylcrotonyl-CoA carboxylase.";
Biochem. Biophys. Res. Commun. 334:939-946(2005).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=17360195; DOI=10.1016/j.pep.2007.01.012;
Chu C.H., Cheng D.;
"Expression, purification, characterization of human 3-methylcrotonyl-
CoA carboxylase (MCCC).";
Protein Expr. Purif. 53:421-427(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
INTERACTION WITH SIRT4.
PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
"Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and
mammals interact with pyruvate carboxylase and other acetylated
biotin-dependent carboxylases.";
Mitochondrion 13:705-720(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
STRUCTURE BY NMR OF 640-725.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-072, an apo-biotinyl domain from human
acetyl coenzyme A carboxylase.";
Submitted (SEP-2007) to the PDB data bank.
[15]
VARIANTS MCC1D LYS-134; PRO-187; TRP-232; VAL-291 AND SER-385, AND
CHARACTERIZATION OF VARIANT MCC1D VAL-291.
PubMed=16010683; DOI=10.1002/humu.9352;
Dantas M.F., Suormala T., Randolph A., Coelho D., Fowler B., Valle D.,
Baumgartner M.R.;
"3-Methylcrotonyl-CoA carboxylase deficiency: mutation analysis in 28
probands, 9 symptomatic and 19 detected by newborn screening.";
Hum. Mutat. 26:164-174(2005).
[16]
VARIANT MCC1D MET-460.
PubMed=17968484; DOI=10.1007/s10038-007-0211-9;
Uematsu M., Sakamoto O., Sugawara N., Kumagai N., Morimoto T.,
Yamaguchi S., Hasegawa Y., Kobayashi H., Ihara K., Yoshino M.,
Watanabe Y., Inokuchi T., Yokoyama T., Kiwaki K., Nakamura K.,
Endo F., Tsuchiya S., Ohura T.;
"Novel mutations in five Japanese patients with 3-methylcrotonyl-CoA
carboxylase deficiency.";
J. Hum. Genet. 52:1040-1043(2007).
[17]
VARIANT MCC1D GLU-46.
PubMed=21071250; DOI=10.1016/j.ymgme.2010.10.008;
Nguyen K.V., Naviaux R.K., Patra S., Barshop B.A., Nyhan W.L.;
"Novel mutations in the human MCCA and MCCB gene causing
methylcrotonylglycinuria.";
Mol. Genet. Metab. 102:218-221(2011).
[18]
VARIANTS MCC1D ARG-276 AND GLN-281.
PubMed=22150417; DOI=10.1111/j.1399-0004.2011.01704.x;
Cho S.Y., Park H.D., Lee Y.W., Ki C.S., Lee S.Y., Sohn Y.B.,
Park S.W., Kim S.H., Ji S., Kim S.J., Choi E.W., Kim C.H., Ko A.R.,
Paik K.H., Lee D.H., Jin D.K.;
"Mutational spectrum in eight Korean patients with 3-methylcrotonyl-
CoA carboxylase deficiency.";
Clin. Genet. 81:96-98(2012).
[19]
VARIANTS MCC1D LYS-56; GLN-281; PRO-380 AND SER-385.
PubMed=22264772; DOI=10.1016/j.ymgme.2011.12.018;
Morscher R.J., Grunert S.C., Burer C., Burda P., Suormala T.,
Fowler B., Baumgartner M.R.;
"A single mutation in MCCC1 or MCCC2 as a potential cause of positive
screening for 3-methylcrotonyl-CoA carboxylase deficiency.";
Mol. Genet. Metab. 105:602-606(2012).
[20]
VARIANTS MCC1D GLU-46; LYS-56; LEU-65; HIS-123; MET-125; LYS-134;
ARG-160; VAL-180; PRO-187; TRP-232; ASP-268; GLN-281; GLY-288;
VAL-289; VAL-291; ARG-325; PRO-372; ASP-379; SER-379; PRO-380;
SER-385; MET-434; MET-439; MET-460; HIS-532; PHE-535 AND
566-VAL-THR-567 DEL, AND CHARACTERIZATION OF VARIANTS MCC1D GLY-288;
ASP-379 AND MET-434.
PubMed=22642865; DOI=10.1186/1750-1172-7-31;
Gruenert S.C., Stucki M., Morscher R.J., Suormala T., Buerer C.,
Burda P., Christensen E., Ficicioglu C., Herwig J., Koelker S.,
Moeslinger D., Pasquini E., Santer R., Schwab K.O., Wilcken B.,
Fowler B., Yue W.W., Baumgartner M.R.;
"3-methylcrotonyl-CoA carboxylase deficiency: clinical, biochemical,
enzymatic and molecular studies in 88 individuals.";
Orphanet J. Rare Dis. 7:31-54(2012).
[21]
VARIANTS MCC1D CYS-79; VAL-209; GLY-288; LYS-366 AND HIS-444.
PubMed=25382614; DOI=10.1111/cge.12535;
Yang L., Yang J., Zhang T., Weng C., Hong F., Tong F., Yang R.,
Yin X., Yu P., Huang X., Qi M.;
"Identification of eight novel mutations and transcript analysis of
two splicing mutations in Chinese newborns with MCC deficiency.";
Clin. Genet. 88:484-488(2015).
[22]
VARIANTS MCC1D PHE-120; SER-130; LYS-383 AND SER-385.
PubMed=27601257; DOI=10.1016/j.gene.2016.09.003;
Fonseca H., Azevedo L., Serrano C., Sousa C., Marcao A., Vilarinho L.;
"3-Methylcrotonyl-CoA carboxylase deficiency: Mutational spectrum
derived from comprehensive newborn screening.";
Gene 594:203-210(2016).
[23]
VARIANT SER-632.
PubMed=28887846; DOI=10.1002/humu.23335;
Zhou X.L., He L.X., Yu L.J., Wang Y., Wang X.J., Wang E.D., Yang T.;
"Mutations in KARS cause early-onset hearing loss and
leukoencephalopathy: Potential pathogenic mechanism.";
Hum. Mutat. 38:1740-1750(2017).
-!- FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA
carboxylase, an enzyme that catalyzes the conversion of 3-
methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
leucine and isovaleric acid catabolism.
{ECO:0000269|PubMed:17360195}.
-!- CATALYTIC ACTIVITY:
Reaction=3-methylbut-2-enoyl-CoA + ATP + hydrogencarbonate = ADP +
H(+) + phosphate + trans-3-methylglutaconyl-CoA;
Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
Evidence={ECO:0000269|PubMed:17360195};
-!- COFACTOR:
Name=biotin; Xref=ChEBI:CHEBI:57586;
-!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-
hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
-!- SUBUNIT: Probably a dodecamer composed of six biotin-containing
alpha subunits (MCCC1) and six beta (MCCC2) subunits
(PubMed:17360195). Interacts (via the biotin carboxylation domain)
with SIRT4 (PubMed:23438705). {ECO:0000269|PubMed:17360195,
ECO:0000269|PubMed:23438705}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:16023992}.
-!- PTM: Acetylated. {ECO:0000250|UniProtKB:Q99MR8}.
-!- DISEASE: 3-methylcrotonoyl-CoA carboxylase 1 deficiency (MCC1D)
[MIM:210200]: An autosomal recessive disorder of leucine
catabolism. The phenotype is variable, ranging from neonatal onset
with severe neurological involvement to asymptomatic adults. There
is a characteristic organic aciduria with massive excretion of 3-
hydroxyisovaleric acid and 3-methylcrotonylglycine, usually in
combination with a severe secondary carnitine deficiency.
{ECO:0000269|PubMed:11170888, ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:11406611, ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:17968484, ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22150417, ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865, ECO:0000269|PubMed:25382614,
ECO:0000269|PubMed:27601257, ECO:0000269|Ref.6}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SEQUENCE CAUTION:
Sequence=BAD92974.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF310972; AAG53095.1; -; mRNA.
EMBL; AB029826; BAA99407.1; -; mRNA.
EMBL; AF297332; AAK67986.1; -; mRNA.
EMBL; AF310339; AAG50245.1; -; mRNA.
EMBL; AK023051; BAB14377.1; -; mRNA.
EMBL; AB209737; BAD92974.1; ALT_INIT; mRNA.
EMBL; BC004214; AAH04214.1; -; mRNA.
EMBL; BC004187; AAH04187.1; -; mRNA.
CCDS; CCDS3241.1; -.
RefSeq; NP_001280202.1; NM_001293273.1.
RefSeq; NP_064551.3; NM_020166.4.
UniGene; Hs.47649; -.
PDB; 2EJM; NMR; -; A=640-725.
PDBsum; 2EJM; -.
ProteinModelPortal; Q96RQ3; -.
SMR; Q96RQ3; -.
BioGrid; 121249; 37.
CORUM; Q96RQ3; -.
IntAct; Q96RQ3; 13.
MINT; Q96RQ3; -.
STRING; 9606.ENSP00000265594; -.
DrugBank; DB00121; Biotin.
iPTMnet; Q96RQ3; -.
PhosphoSitePlus; Q96RQ3; -.
SwissPalm; Q96RQ3; -.
BioMuta; MCCC1; -.
DMDM; 108861983; -.
EPD; Q96RQ3; -.
jPOST; Q96RQ3; -.
MaxQB; Q96RQ3; -.
PaxDb; Q96RQ3; -.
PeptideAtlas; Q96RQ3; -.
PRIDE; Q96RQ3; -.
ProteomicsDB; 78003; -.
Ensembl; ENST00000265594; ENSP00000265594; ENSG00000078070.
GeneID; 56922; -.
KEGG; hsa:56922; -.
UCSC; uc003fle.4; human.
CTD; 56922; -.
DisGeNET; 56922; -.
EuPathDB; HostDB:ENSG00000078070.11; -.
GeneCards; MCCC1; -.
HGNC; HGNC:6936; MCCC1.
HPA; HPA008310; -.
MalaCards; MCCC1; -.
MIM; 210200; phenotype.
MIM; 609010; gene.
neXtProt; NX_Q96RQ3; -.
OpenTargets; ENSG00000078070; -.
Orphanet; 6; 3-methylcrotonyl-CoA carboxylase deficiency.
PharmGKB; PA30680; -.
eggNOG; KOG0238; Eukaryota.
eggNOG; COG4770; LUCA.
GeneTree; ENSGT00940000156941; -.
HOGENOM; HOG000008989; -.
HOVERGEN; HBG000555; -.
InParanoid; Q96RQ3; -.
KO; K01968; -.
OMA; NVHTNFI; -.
OrthoDB; 254436at2759; -.
PhylomeDB; Q96RQ3; -.
TreeFam; TF105650; -.
BioCyc; MetaCyc:ENSG00000078070-MONOMER; -.
Reactome; R-HSA-196780; Biotin transport and metabolism.
Reactome; R-HSA-3371599; Defective HLCS causes multiple carboxylase deficiency.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
UniPathway; UPA00363; UER00861.
ChiTaRS; MCCC1; human.
EvolutionaryTrace; Q96RQ3; -.
GenomeRNAi; 56922; -.
PRO; PR:Q96RQ3; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000078070; Expressed in 218 organ(s), highest expression level in body of pancreas.
ExpressionAtlas; Q96RQ3; baseline and differential.
Genevisible; Q96RQ3; HS.
GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; TAS:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005759; C:mitochondrial matrix; IDA:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009374; F:biotin binding; NAS:UniProtKB.
GO; GO:0004075; F:biotin carboxylase activity; NAS:ParkinsonsUK-UCL.
GO; GO:0046872; F:metal ion binding; IEA:InterPro.
GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
GO; GO:0006552; P:leucine catabolic process; ISS:ParkinsonsUK-UCL.
GO; GO:0051291; P:protein heterooligomerization; NAS:ParkinsonsUK-UCL.
Gene3D; 3.30.1490.20; -; 1.
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; IPR016185; PreATP-grasp_dom_sf.
InterPro; IPR011054; Rudment_hybrid_motif.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF02785; Biotin_carb_C; 1.
Pfam; PF00289; Biotin_carb_N; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF02786; CPSase_L_D2; 1.
SMART; SM00878; Biotin_carb_C; 1.
SUPFAM; SSF51230; SSF51230; 1.
SUPFAM; SSF51246; SSF51246; 1.
SUPFAM; SSF52440; SSF52440; 1.
PROSITE; PS50975; ATP_GRASP; 1.
PROSITE; PS50979; BC; 1.
PROSITE; PS00188; BIOTIN; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS00867; CPSASE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Biotin; Complete proteome;
Direct protein sequencing; Disease mutation; Ligase; Mitochondrion;
Nucleotide-binding; Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 41 Mitochondrion.
{ECO:0000269|PubMed:16023992}.
CHAIN 42 725 Methylcrotonoyl-CoA carboxylase subunit
alpha, mitochondrial.
/FTId=PRO_0000002833.
DOMAIN 48 494 Biotin carboxylation.
DOMAIN 167 364 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
DOMAIN 643 715 Biotinyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
ACT_SITE 339 339 {ECO:0000250}.
BINDING 163 163 ATP. {ECO:0000250}.
BINDING 247 247 ATP. {ECO:0000250}.
BINDING 282 282 ATP. {ECO:0000250}.
MOD_RES 237 237 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 581 581 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 581 581 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q99MR8}.
MOD_RES 681 681 N6-biotinyllysine. {ECO:0000250,
ECO:0000255|PROSITE-ProRule:PRU01066}.
VARIANT 46 46 G -> E (in MCC1D; dbSNP:rs199517715).
{ECO:0000269|PubMed:21071250,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072486.
VARIANT 56 56 N -> K (in MCC1D; dbSNP:rs1057520695).
{ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072487.
VARIANT 65 65 M -> L (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072488.
VARIANT 79 79 Y -> C (in MCC1D).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077284.
VARIANT 120 120 S -> F (in MCC1D).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077285.
VARIANT 123 123 Q -> H (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072489.
VARIANT 125 125 I -> M (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072490.
VARIANT 130 130 G -> S (in MCC1D; clinically asymptomatic
form; dbSNP:rs202197951).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077286.
VARIANT 134 134 E -> K (in MCC1D; dbSNP:rs1229069160).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072491.
VARIANT 160 160 M -> R (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072492.
VARIANT 180 180 G -> V (in MCC1D; dbSNP:rs748201122).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072493.
VARIANT 187 187 S -> P (in MCC1D; dbSNP:rs757362635).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072494.
VARIANT 209 209 G -> V (in MCC1D; dbSNP:rs186209189).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077287.
VARIANT 232 232 R -> W (in MCC1D; dbSNP:rs727504004).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072495.
VARIANT 268 268 A -> D (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072496.
VARIANT 276 276 C -> R (in MCC1D; dbSNP:rs773433541).
{ECO:0000269|PubMed:22150417}.
/FTId=VAR_067197.
VARIANT 281 281 R -> Q (in MCC1D; dbSNP:rs754437245).
{ECO:0000269|PubMed:22150417,
ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_067198.
VARIANT 288 288 E -> G (in MCC1D; shows no residual
activity; dbSNP:rs746500530).
{ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:25382614}.
/FTId=VAR_072497.
VARIANT 289 289 A -> V (in MCC1D; mild form;
dbSNP:rs1326114075).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012785.
VARIANT 291 291 A -> V (in MCC1D; associated with a
reduction of wild-type residual activity;
dbSNP:rs201041864).
{ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072498.
VARIANT 325 325 M -> R (in MCC1D; dbSNP:rs119103212).
{ECO:0000269|PubMed:11170888,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012786.
VARIANT 366 366 E -> K (in MCC1D; unknown pathological
significance; dbSNP:rs201386261).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077288.
VARIANT 372 372 Q -> P (in MCC1D; dbSNP:rs755328329).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072499.
VARIANT 379 379 G -> D (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072500.
VARIANT 379 379 G -> S (in MCC1D; dbSNP:rs887877405).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072501.
VARIANT 380 380 H -> P (in MCC1D; dbSNP:rs794727036).
{ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072502.
VARIANT 383 383 E -> K (in MCC1D; unknown pathological
significance; dbSNP:rs1333357031).
{ECO:0000269|PubMed:27601257}.
/FTId=VAR_077289.
VARIANT 385 385 R -> S (in MCC1D; severe form;
dbSNP:rs119103213).
{ECO:0000269|PubMed:11170888,
ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:16010683,
ECO:0000269|PubMed:22264772,
ECO:0000269|PubMed:22642865,
ECO:0000269|PubMed:27601257}.
/FTId=VAR_012787.
VARIANT 434 434 I -> M (in MCC1D; shows some wild-type
residual activity; dbSNP:rs376289130).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072503.
VARIANT 437 437 L -> P (in MCC1D; severe form;
dbSNP:rs119103215).
{ECO:0000269|PubMed:11181649}.
/FTId=VAR_012788.
VARIANT 439 439 V -> M (in MCC1D; dbSNP:rs398124352).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072504.
VARIANT 444 444 R -> H (in MCC1D; dbSNP:rs768785753).
{ECO:0000269|PubMed:25382614}.
/FTId=VAR_077290.
VARIANT 460 460 I -> M (in MCC1D; dbSNP:rs119103218).
{ECO:0000269|PubMed:17968484,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_072505.
VARIANT 464 464 H -> P (in dbSNP:rs2270968).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:11406611,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_012789.
VARIANT 532 532 D -> H (in MCC1D; severe form;
dbSNP:rs119103214).
{ECO:0000269|PubMed:11181649,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012790.
VARIANT 535 535 S -> F (in MCC1D; asymptomatic form;
dbSNP:rs119103216).
{ECO:0000269|PubMed:11406611,
ECO:0000269|PubMed:22642865}.
/FTId=VAR_012791.
VARIANT 560 560 N -> T (in dbSNP:rs35219417).
/FTId=VAR_038631.
VARIANT 566 567 Missing (in MCC1D).
{ECO:0000269|PubMed:22642865}.
/FTId=VAR_072506.
VARIANT 632 632 P -> S (in dbSNP:rs142867987).
{ECO:0000269|PubMed:28887846}.
/FTId=VAR_079752.
CONFLICT 469 469 F -> L (in Ref. 3; AAK67986).
{ECO:0000305}.
STRAND 652 660 {ECO:0000244|PDB:2EJM}.
STRAND 666 668 {ECO:0000244|PDB:2EJM}.
STRAND 673 687 {ECO:0000244|PDB:2EJM}.
STRAND 692 698 {ECO:0000244|PDB:2EJM}.
STRAND 703 705 {ECO:0000244|PDB:2EJM}.
STRAND 712 714 {ECO:0000244|PDB:2EJM}.
SEQUENCE 725 AA; 80473 MW; B84AD23806035A40 CRC64;
MAAASAVSVL LVAAERNRWH RLPSLLLPPR TWVWRQRTMK YTTATGRNIT KVLIANRGEI
ACRVMRTAKK LGVQTVAVYS EADRNSMHVD MADEAYSIGP APSQQSYLSM EKIIQVAKTS
AAQAIHPGCG FLSENMEFAE LCKQEGIIFI GPPPSAIRDM GIKSTSKSIM AAAGVPVVEG
YHGEDQSDQC LKEHARRIGY PVMIKAVRGG GGKGMRIVRS EQEFQEQLES ARREAKKSFN
DDAMLIEKFV DTPRHVEVQV FGDHHGNAVY LFERDCSVQR RHQKIIEEAP APGIKSEVRK
KLGEAAVRAA KAVNYVGAGT VEFIMDSKHN FCFMEMNTRL QVEHPVTEMI TGTDLVEWQL
RIAAGEKIPL SQEEITLQGH AFEARIYAED PSNNFMPVAG PLVHLSTPRA DPSTRIETGV
RQGDEVSVHY DPMIAKLVVW AADRQAALTK LRYSLRQYNI VGLHTNIDFL LNLSGHPEFE
AGNVHTDFIP QHHKQLLLSR KAAAKESLCQ AALGLILKEK AMTDTFTLQA HDQFSPFSSS
SGRRLNISYT RNMTLKDGKN NVAIAVTYNH DGSYSMQIED KTFQVLGNLY SEGDCTYLKC
SVNGVASKAK LIILENTIYL FSKEGSIEID IPVPKYLSSV SSQETQGGPL APMTGTIEKV
FVKAGDKVKA GDSLMVMIAM KMEHTIKSPK DGTVKKVFYR EGAQANRHTP LVEFEEEESD
KRESE


Related products :

Catalog number Product name Quantity
15-288-21224 Propionyl-CoA carboxylase alpha chain. mitochondrial - EC 6.4.1.3; PCCase subunit alpha; Propanoyl-CoA carbon dioxide ligase subunit alpha Polyclonal 0.05 mg
15-288-21224 Propionyl-CoA carboxylase alpha chain. mitochondrial - EC 6.4.1.3; PCCase subunit alpha; Propanoyl-CoA carbon dioxide ligase subunit alpha Polyclonal 0.1 mg
EIAAB30041 Pcca,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial,Rat,Rattus norvegicus
EIAAB30042 Mouse,Mus musculus,Pcca,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial
EIAAB30040 Homo sapiens,Human,PCCA,PCCase subunit alpha,Propanoyl-CoA carbon dioxide ligase subunit alpha,Propionyl-CoA carboxylase alpha chain, mitochondrial
EIAAB30046 PCCase subunit beta,PCCB,Pig,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Sus scrofa
EIAAB30044 PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial,Rat,Rattus norvegicus
EIAAB30045 Bos taurus,Bovine,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30047 Mouse,Mus musculus,PCCase subunit beta,Pccb,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
EIAAB30043 Homo sapiens,Human,PCCase subunit beta,PCCB,Propanoyl-CoA carbon dioxide ligase subunit beta,Propionyl-CoA carboxylase beta chain, mitochondrial
E0195h Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
CSB-EL013572RA Rat Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit 96T
STOX1_HUMAN Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
HCST_MOUSE Human ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial 96T
CSB-EL013572MO Mouse Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit 96T
CSB-EL013572HU Human Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit 96T
CSB-EL013572RA Rat Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit SpeciesRat 96T
CSB-EL013572MO Mouse Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit SpeciesMouse 96T
CSB-EL013572HU Human Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial(MCCC1) ELISA kit SpeciesHuman 96T
MCCA_MOUSE ELISA Kit FOR Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; organism: Mouse; gene name: Mccc1 96T
U1345m CLIA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345m ELISA Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
E1345m ELISA kit Epiligrin subunit alpha,Kalinin subunit alpha,Lama3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alpha,Mouse,Mus musculus,Nicein subunit alpha 96T
U1345h CLIA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit alp 96T
E1345h ELISA E170,Epiligrin 170 kDa subunit,Epiligrin subunit alpha,Homo sapiens,Human,Kalinin subunit alpha,LAMA3,Laminin subunit alpha-3,Laminin-5 subunit alpha,Laminin-6 subunit alpha,Laminin-7 subunit al 96T

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP296: TCA Cycle - biocyc
WP1566: Citrate cycle (TCA cycle)
WP1614: 1- and 2-Methylnaphthalene degradation
WP1655: Geraniol degradation
WP1671: Methane metabolism
WP1672: Mismatch repair
WP1711: Trinitrotoluene degradation
WP1493: Carbon assimilation C4 pathway
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1644: DNA replication
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
WP1693: Purine metabolism
WP1694: Pyrimidine metabolism
WP1718: Vitamin B6 metabolism
WP2272: Pathogenic Escherichia coli infection
WP2292: Chemokine signaling pathway
WP1003: Ovarian Infertility Genes
WP1047: TNF-alpha NF-kB Signaling Pathway
WP1120: Ovarian Infertility Genes
WP1163: TNF-alpha NF-kB Signaling Pathway
WP1209: EBV LMP1 signaling
WP1224: EBV LMP1 signaling
WP1225: estrogen signalling

Related Genes :
[MCCC1 MCCA] Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial (MCCase subunit alpha) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 1) (3-methylcrotonyl-CoA carboxylase biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha)
[MCCC2 MCCB] Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial (MCCase subunit beta) (EC 6.4.1.4) (3-methylcrotonyl-CoA carboxylase 2) (3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit) (3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta)
[HLCS] Biotin--protein ligase (EC 6.3.4.-) (Biotin apo-protein ligase) [Includes: Biotin--[methylmalonyl-CoA-carboxytransferase] ligase (EC 6.3.4.9); Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase (EC 6.3.4.10) (Holocarboxylase synthetase) (HCS); Biotin--[methylcrotonoyl-CoA-carboxylase] ligase (EC 6.3.4.11); Biotin--[acetyl-CoA-carboxylase] ligase (EC 6.3.4.15)]
[PCCB] Propionyl-CoA carboxylase beta chain, mitochondrial (PCCase subunit beta) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit beta)
[ACC1 ABP2 FAS3 MTR7 YNR016C N3175] Acetyl-CoA carboxylase (ACC) (EC 6.4.1.2) (Fatty acid synthetase 3) (mRNA transport-defective protein 7) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[accA b0185 JW0180] Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (ACCase subunit alpha) (Acetyl-CoA carboxylase carboxyltransferase subunit alpha) (EC 2.1.3.15)
[Acaca Acac] Acetyl-CoA carboxylase 1 (ACC1) (EC 6.4.1.2) (ACC-alpha) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[ACC1 EMB22 GK PAS3 At1g36160 F15C21.1] 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)]
[Acacb Acc2 Accb] Acetyl-CoA carboxylase 2 (EC 6.4.1.2) (ACC-beta) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[CAC2 At5g35360 T26D22.8] Biotin carboxylase, chloroplastic (EC 6.3.4.14) (Acetyl-CoA carboxylase subunit A) (ACC) (EC 6.4.1.2)
[SUCLG1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[SUCLG1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[Prkaa1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[HFA1 YMR207C YM8261.01C YM8325.08C] Acetyl-CoA carboxylase, mitochondrial (ACC) (EC 6.4.1.2) [Includes: Biotin carboxylase (EC 6.3.4.14)]
[Suclg1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[Scsalpha1 Scsalpha CG1065] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (Succinyl-coenzyme A synthetase alpha subunit 1)
[scsA DDB_G0289325] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) (p36)
[accD dedB usg b2316 JW2313] Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 2.1.3.15)
[Prkaa1 Ampk1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[Prkaa2] 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)
[birA bioR dhbB b3973 JW3941] Bifunctional ligase/repressor BirA (Biotin operon repressor) (Biotin--[acetyl-CoA-carboxylase] ligase) (EC 6.3.4.15) (Biotin--protein ligase) (Biotin-[acetyl-CoA carboxylase] synthetase)
[PRKAA1 AMPK1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[] 4-chlorobenzoyl coenzyme A dehalogenase (4-CBA-CoA dehalogenase) (4-CBCoA dehalogenase) (4-chlorobenzoyl-CoA dehalogenase) (EC 3.8.1.7)
[accD ycf11 zfpA] Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 2.1.3.15)
[PRKAA1 AMPK1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (AMPK 63 kDa subunit) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26) (Fragments)
[Suclg1] Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)
[PRKAA1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26) (Fragment)
[HADHA HADH] Trifunctional enzyme subunit alpha, mitochondrial (78 kDa gastrin-binding protein) (TP-alpha) [Includes: Long-chain enoyl-CoA hydratase (EC 4.2.1.17); Long chain 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211)]
[PRKAA2 AMPK AMPK2] 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)
[Prkaa2 Ampk Ampk2] 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)

Bibliography :
?>