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Database: UniProt
Entry: K1VAC0_TRIAC
LinkDB: K1VAC0_TRIAC
Original site: K1VAC0_TRIAC 
ID   K1VAC0_TRIAC            Unreviewed;       585 AA.
AC   K1VAC0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 39.
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:carbon dioxide ligase subunit beta {ECO:0000256|ARBA:ARBA00031237};
GN   ORFNames=A1Q2_04721 {ECO:0000313|EMBL:EKD00980.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD00980.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD00980.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD00980.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKD00980.1}.
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DR   EMBL; AMBO01000329; EKD00980.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1VAC0; -.
DR   STRING; 1220162.K1VAC0; -.
DR   eggNOG; KOG0540; Eukaryota.
DR   HOGENOM; CLU_018822_0_1_1; -.
DR   InParanoid; K1VAC0; -.
DR   OMA; AYLPIMS; -.
DR   OrthoDB; 5474505at2759; -.
DR   UniPathway; UPA00363; UER00861.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
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; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757}.
FT   DOMAIN          59..317
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          321..555
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          28..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  62467 MW;  260C5CA8FCA80BBE CRC64;
     MMLRARTRVA PTVARAGNLN LARTLIAQPP TLPNNAPPSP LPTKLKPNDP ETKEAKANMT
     NLVENLKALR AKAREGGGKK TLEKWKAKGQ GKLSARERVQ ALLDPDSAFL ELSPLAAHEV
     YPDDLPGAGI ITGIGTVSGT RCMIIANDPT VKGGAYYPLT VKKHLRAQQV ALENRLPCVY
     LVESGGAALP YQSNVFPDHD HFGRIFYNMA RMSGLGIPQI SVTHGISVAG GAYMPAMSDV
     VIIVKNQGRI FLAGPPLVKA ATGEVVDDET LGGGDMHTSV SGVADYLAQN DAHAIRLARE
     AVLDLGKATV PSAKAPRETR EPAYPAEELN SIVPADSRKS FDMKEVIARI TDGSEFREFK
     KEYGKTVITG FAEIHGHTVG IVANNGVLLS PSALKATHFI ELCNQRGIPL VFLVNVSGYM
     VGQAAERGGI AKDGAKMVRA VARAKVPKFT VVVNGSYGAG NYGMCGRAYS PRFLFMWPNA
     KVCVMGPDQL SSVMQTVSGN RNAADAEKKF AELRARIEKE SEALYSTARL WDDGIIQPSD
     TRDVLGLALE VAADEKASRP QGGNGGSRGE IGADGDSGDW GVFRM
//
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