MCCB_CAEEL
ID MCCB_CAEEL Reviewed; 608 AA.
AC P34385;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial;
DE Short=MCCase subunit beta;
DE EC=6.4.1.4 {ECO:0000250|UniProtKB:Q9HCC0};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 2;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit;
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta;
DE Flags: Precursor;
GN ORFNames=F02A9.10 {ECO:0000312|WormBase:F02A9.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Carboxyltransferase 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. {ECO:0000250|UniProtKB:Q9HCC0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-
CC methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
CC Evidence={ECO:0000250|UniProtKB:Q9HCC0};
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC {ECO:0000250|UniProtKB:Q9HCC0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q9HCC0}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; BX284603; CAA79618.1; -; Genomic_DNA.
DR PIR; S28313; S28313.
DR RefSeq; NP_499013.1; NM_066612.4.
DR AlphaFoldDB; P34385; -.
DR SMR; P34385; -.
DR BioGRID; 41484; 4.
DR STRING; 6239.F02A9.4a; -.
DR EPD; P34385; -.
DR PaxDb; P34385; -.
DR PeptideAtlas; P34385; -.
DR EnsemblMetazoa; F02A9.10.1; F02A9.10.1; WBGene00303021.
DR GeneID; 41656988; -.
DR UCSC; F02A9.4b; c. elegans.
DR CTD; 41656988; -.
DR WormBase; F02A9.10; CE00136; WBGene00303021; -.
DR eggNOG; KOG0540; Eukaryota.
DR GeneTree; ENSGT00940000155949; -.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; P34385; -.
DR OMA; AYLPIMS; -.
DR OrthoDB; 632665at2759; -.
DR PhylomeDB; P34385; -.
DR Reactome; R-CEL-196780; Biotin transport and metabolism.
DR Reactome; R-CEL-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00363; UER00861.
DR PRO; PR:P34385; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00303021; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; HDA:WormBase.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; PTHR22855; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 62..608
FT /note="Probable methylcrotonoyl-CoA carboxylase beta chain,
FT mitochondrial"
FT /id="PRO_0000199804"
FT DOMAIN 94..351
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 351..600
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 94..600
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 388..417
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 608 AA; 66524 MW; 2502FB70D987B6E0 CRC64;
MFRHVAQNLG SRNTSIQSYR LLRTRWERGY LKDLYHRRQI LGADPAISRS SYPNCSVQVR
NHHCSADKST LQWAPIKTSI DNSSDDFAAN TAEMKVLVED LKAKISKIEQ AGGEKAVKLH
RSRGKMLARE RIDGIVDAGS PFIEFSQLAG YEMYGKEEVP SGGILTGVGI VSGRVCVIVA
NDATVKGGTY YPITVKKHLR AQEIARENKL PCIYLVDSGG ANLPRQADIF ADSQHFGRIF
YNQATMSSEG IPQLAVVMGS CTAGGAYVPA MSDQAIIVKG TGTVFLGGPP LVKAATGEEI
SAEELGGADL HCGESGVTDY YAHNDKHALY LARSCIAGLP PVEEHMTFNP NADEPLYPAE
EIYGIVGSNL KKTYDVREVI ARIVDGSRFH EFKERYGETL VTGFATIYGQ RVGILANNGV
LFAESAMKGS HFIELCCQRK IPLLFLQNIT GFMVGRDAEA GGIAKHGAKL VTAVACAKVP
KITVLVGGSY GAGNYGMCGR GYSPRYVFMW PNSRISVMGG EQAANVLSTV QKEKKKREGA
DWTDQQDLEL RKPVEEKFEK EGHPYFASAR LWDDGVIDPK DTRKVLGLAF QSTLQKPIPE
TKFGVFRM
