ID Q8AXQ5_PAGMA Unreviewed; 198 AA.
AC Q8AXQ5;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=methylcrotonoyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00026116};
DE EC=6.4.1.4 {ECO:0000256|ARBA:ARBA00026116};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 2 {ECO:0000256|ARBA:ARBA00031404};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit {ECO:0000256|ARBA:ARBA00031109};
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta {ECO:0000256|ARBA:ARBA00031237};
DE Flags: Fragment;
GN Name=MCCC2 {ECO:0000313|EMBL:BAC44999.1};
OS Pagrus major (Red sea bream) (Chrysophrys major).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Spariformes; Sparidae; Pagrus.
OX NCBI_TaxID=143350 {ECO:0000313|EMBL:BAC44999.1};
RN [1] {ECO:0000313|EMBL:BAC44999.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:BAC44999.1};
RA Abe S., Chamnan C., Miyamoto K., Minamino Y., Nouda M.;
RT "Isolation and identification of pyruvate carboxylase and 3-methylcrotonyl
RT CoA carboxylase cDNAs and their expression in Sea bream (Pagrus major)
RT organs.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAC44999.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver {ECO:0000313|EMBL:BAC44999.1};
RA Abe S., Miyamoto K., Minamino Y.;
RT "Pagrus major 3-methylcrotonyl CoA carboxylase non-biotin containing
RT subunit mRNA, partial cds.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00029358};
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}.
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DR EMBL; AB082535; BAC44999.1; -; mRNA.
DR AlphaFoldDB; Q8AXQ5; -.
DR UniPathway; UPA00363; UER00861.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
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; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 2: Evidence at transcript level;
FT DOMAIN 1..67
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 70..198
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAC44999.1"
FT NON_TER 198
FT /evidence="ECO:0000313|EMBL:BAC44999.1"
SQ SEQUENCE 198 AA; 21501 MW; 860E05A10804D249 CRC64;
FLGGPPLVKA ATGEEVSAED LGGADLHCKK SGVTDHYALD DNHALHLARK AVRSLNYRKN
IEVTTEPTEA PLYPADELYG IVGDNLKRNF DVREVIARIV DGSKFDEFKA FYGDTLVTGF
SRIFGYPVGI IGNNGVLFSE SAKKGTHFIE LCCQRNIPLI FLQNITGFMV GREYEAGGIA
KDGAKMVTAV ACANVPKM
//
