MCCB_RAT
ID MCCB_RAT Reviewed; 563 AA.
AC Q5XIT9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial;
DE Short=MCCase subunit beta;
DE EC=6.4.1.4;
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 Name=Mccc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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 -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC subunits (MCCC1) and six beta (MCCC2) subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; BC083581; AAH83581.1; -; mRNA.
DR RefSeq; NP_001012177.1; NM_001012177.1.
DR AlphaFoldDB; Q5XIT9; -.
DR SMR; Q5XIT9; -.
DR BioGRID; 263035; 2.
DR IntAct; Q5XIT9; 1.
DR STRING; 10116.ENSRNOP00000023900; -.
DR iPTMnet; Q5XIT9; -.
DR PhosphoSitePlus; Q5XIT9; -.
DR jPOST; Q5XIT9; -.
DR PaxDb; Q5XIT9; -.
DR PRIDE; Q5XIT9; -.
DR Ensembl; ENSRNOT00000023900; ENSRNOP00000023900; ENSRNOG00000017752.
DR GeneID; 361884; -.
DR KEGG; rno:361884; -.
DR UCSC; RGD:1310279; rat.
DR CTD; 64087; -.
DR RGD; 1310279; Mccc2.
DR eggNOG; KOG0540; Eukaryota.
DR GeneTree; ENSGT00940000155949; -.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; Q5XIT9; -.
DR OMA; AYLPIMS; -.
DR OrthoDB; 632665at2759; -.
DR PhylomeDB; Q5XIT9; -.
DR TreeFam; TF300446; -.
DR Reactome; R-RNO-196780; Biotin transport and metabolism.
DR Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00363; UER00861.
DR PRO; PR:Q5XIT9; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000017752; Expressed in stomach and 20 other tissues.
DR Genevisible; Q5XIT9; RN.
DR GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; ISO:RGD.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
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:0015936; P:coenzyme A metabolic process; IDA:RGD.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 23..563
FT /note="Methylcrotonoyl-CoA carboxylase beta chain,
FT mitochondrial"
FT /id="PRO_0000284069"
FT DOMAIN 49..306
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 309..555
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 49..555
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 343..372
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT MOD_RES 70
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3ULD5"
FT MOD_RES 70
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3ULD5"
FT MOD_RES 141
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3ULD5"
FT MOD_RES 433
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3ULD5"
FT MOD_RES 495
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3ULD5"
FT MOD_RES 495
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q3ULD5"
FT MOD_RES 511
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3ULD5"
SQ SEQUENCE 563 AA; 61517 MW; B9BEB34E88B2D148 CRC64;
MWGALRSVLR PCSRASVPRQ RAYHGDAVAR LGTQPDSGSS TYQENYEQMK ALVNQLHERA
QYVRLGGSEK ARARHTSRGK LLPRDRIDNL IDPGSPFLEF SQFAGYKLYG EEEVPAGGII
TGIGRVSGVE CMIVANDATV KGGTYYPVTV KKHVRAQEIA LQNRLPCIYL VDSGGANLPR
QADTFPDRDH FGRIFYNQAI MSSKNITQIA VVMGSCTAGG AYVPAMADEN IIVQRQGTIF
LAGPPLVKAA TGEEVSAEDL GGADLHCRRS GVTDHYALDD HHALHLTRKV VRSLNYQKKL
DVTVEPSEEP LFPADELYGI VGANLKRSFD VREVIARIVD GSRFNEFKAL YGDTLVTGFA
RIFGYPVGII GNNGVLFSES AKKGAHFVQL CCQRNIPLLF LQNITGFMVG KDYEAEGIAK
DGAKMVAAVS CAKVPKITVI IGGSYGAGNY GMCGRAYSPR FLYMWPNARI SVMGGEQAAT
VLATVARDQR AREGKQFSSA EEAALKEPII KRFEEEGNPY YSSARLWDDG IIDPVDTRLV
LGLSISAALN APIQRTDFGI FRM
