ID A0A4W4FP51_ELEEL Unreviewed; 689 AA.
AC A0A4W4FP51;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2025, sequence version 2.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0000256|ARBA:ARBA00070568};
DE EC=6.4.1.4 {ECO:0000256|ARBA:ARBA00026116};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 1 {ECO:0000256|ARBA:ARBA00076115};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit {ECO:0000256|ARBA:ARBA00076418};
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha {ECO:0000256|ARBA:ARBA00082627};
GN Name=MCCC1 {ECO:0000313|Ensembl:ENSEEEP00000025709.2};
OS Electrophorus electricus (Electric eel) (Gymnotus electricus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Gymnotiformes;
OC Gymnotoidei; Gymnotidae; Electrophorus.
OX NCBI_TaxID=8005 {ECO:0000313|Ensembl:ENSEEEP00000025709.2, ECO:0000313|Proteomes:UP000314983};
RN [1] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24970089;
RA Gallant J.R., Traeger L.L., Volkening J.D., Moffett H., Chen P.H.,
RA Novina C.D., Phillips G.N.Jr., Anand R., Wells G.B., Pinch M., Guth R.,
RA Unguez G.A., Albert J.S., Zakon H.H., Samanta M.P., Sussman M.R.;
RT "Nonhuman genetics. Genomic basis for the convergent evolution of electric
RT organs.";
RL Science 344:1522-1525(2014).
RN [2] {ECO:0000313|Proteomes:UP000314983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28695212;
RA Traeger L.L., Sabat G., Barrett-Wilt G.A., Wells G.B., Sussman M.R.;
RT "A tail of two voltages: Proteomic comparison of the three electric organs
RT of the electric eel.";
RL Sci. Adv. 3:e1700523-e1700523(2017).
RN [3] {ECO:0000313|Ensembl:ENSEEEP00000025709.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Myers G., Meyer A., Fedrigo O., Formenti G., Rhie A., Tracey A., Sims Y.,
RA Jarvis E.D.;
RT "Electrophorus electricus (electric eel) genome, fEleEle1, primary
RT haplotype.";
RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSEEEP00000025709.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [5] {ECO:0000313|Ensembl:ENSEEEP00000025709.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Biotin-attachment subunit of the 3-methylcrotonyl-CoA
CC carboxylase, an enzyme that catalyzes the conversion of 3-
CC methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
CC leucine and isovaleric acid catabolism.
CC {ECO:0000256|ARBA:ARBA00055202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methylbut-2-enoyl-CoA + hydrogencarbonate + ATP = 3-methyl-
CC (2E)-glutaconyl-CoA + ADP + phosphate + H(+); Xref=Rhea:RHEA:13589,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57344, ChEBI:CHEBI:57346,
CC ChEBI:CHEBI:456216; EC=6.4.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00052347};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC {ECO:0000256|ARBA:ARBA00025711}.
CC -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC subunits (MCCC1) and six beta (MCCC2) subunits. Interacts (via the
CC biotin carboxylation domain) with SIRT4.
CC {ECO:0000256|ARBA:ARBA00065291}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
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DR AlphaFoldDB; A0A4W4FP51; -.
DR Ensembl; ENSEEET00000026005.2; ENSEEEP00000025709.2; ENSEEEG00000011984.2.
DR GeneTree; ENSGT00940000156941; -.
DR Proteomes; UP000314983; Chromosome 26.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR CDD; cd06850; biotinyl_domain; 1.
DR FunFam; 2.40.50.100:FF:000003; Acetyl-CoA carboxylase biotin carboxyl carrier protein; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.30.470.20:FF:000028; Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR050856; Biotin_carboxylase_complex.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CPAse_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000314983};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 29..475
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 148..345
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 601..679
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 689 AA; 76247 MW; 3340BFF95F4514E1 CRC64;
ALSENALETL YKTVATKLQS RRHFLSTGRM EKVLIANRGE IACRVMRTAR KMGVRSVAVY
SDADRHSMHV AMADEAYHIG ASPSQQSYLC MEKVLEVAKK SSAQAIHPGY GFLSENTEFA
ELCKQEGILF IGPPSSAIRD MGIKSTSKHI MSAAGVPIIE GYHGEDQSDE RLQAEATRIG
YPVMIKAVRG GGGKGMRIAR SEADFHQQLE SARREACKSF NDDVMLVEKF VENPRHVEVQ
VFGDQHGNAV YLFERDCSVQ RRHQKIIEEA PGPGISPEVR RKLGEAAVQA AKAVNYVGAG
TVEFIMDAQH NFYFMEMNTR LQVEHPVSEM ITGTDLVEWQ LRVTAGEKLP LSQEEIVLRG
HSFEARIYAE DPANDFLPGA GPLLHLSTPQ ADEHTRIETG VREGDEVSAH YDPMIAKLVV
WGKDRSAALK KLRYCLRQYN IVGLNTNIDF LLSLSGHPCF ESGDVHTSFI PQHYEQLFPP
PAQASVEETC QAALGLLLHE KEHTREFTRR SHDMYSPFGL GDGTRLNVLY CRNLRLHLGT
NSECQGFQVS GELQKEGGAT YLHCCVNGVL SRPKLVILDN TVHLFSTEGS AQVNVPLPKF
LAGVSTSGAQ DGAVAPMTGT IEKVLIQVGD TVHKGDPLMV MIAMKMEHTI RAPKAGVIKK
VFFKEGAQAN RHAPLVELKE EEQEEQPQP
//
