ID A0A010S2I2_9PEZI Unreviewed; 1217 AA.
AC A0A010S2I2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=CFIO01_01617 {ECO:0000313|EMBL:EXF78778.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78778.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF78778.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF78778.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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}.
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:EXF78778.1}.
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DR EMBL; JARH01000609; EXF78778.1; -; Genomic_DNA.
DR RefSeq; XP_007597561.1; XM_007597499.1.
DR AlphaFoldDB; A0A010S2I2; -.
DR STRING; 1445577.A0A010S2I2; -.
DR KEGG; cfj:CFIO01_01617; -.
DR eggNOG; KOG0540; Eukaryota.
DR eggNOG; KOG1681; Eukaryota.
DR eggNOG; KOG2368; Eukaryota.
DR HOGENOM; CLU_269064_0_0_1; -.
DR OrthoDB; 1210873at2759; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000020467; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd06558; crotonase-like; 1.
DR CDD; cd07938; DRE_TIM_HMGL; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR PANTHER; PTHR22855:SF46; METHYLCROTONOYL-COA CARBOXYLASE; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF00378; ECH_1; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 3.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:EXF78778.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020467}.
FT DOMAIN 1..242
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 258..497
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT DOMAIN 621..895
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 1217 AA; 132506 MW; 1D0F0D464497C99E CRC64;
MIEQLFPVEK STVDLTASNF QANRQAWEPV LREFDNYLKD VSSEGDEAST SRHQTRHQLL
RIGLVSQRPC LLLSHIPTQS GGAWNEMTVL KVNRILEIGF ENDLPLISLV QSAGVFLPQQ
FRVFHKGGQL FRDLAIRSQQ GKPSCAIVFG SSTAGGAYHP ALSDYTIFVE NQAQVFLGGP
PLVKMATSEV VTAEELGGAK IHASTTGLAD QIAMDEFDAI QKAREWVATL RTPEPSRLLT
ISSHPVPPRY SIDDLLYLVN TDIRKPFDMR EVLLRLVDDS RMSIFKPSYG TNMLTAWADI
FGFRAGIVAN QTPVIHPHEA LKAAQFIRLC NQENTPIVFL HNVTGFMVGT KAEHSGIIKA
GAQLVSAVSC STVPHISIIL GASYGAGNYA MCGRSYRPRF LFTWPTGRCS VMGPDQLAGV
VETIRTKSNG GSKLSPDEIK AQAAQLREDA YRDSTSYATS SMLIDDGIID PRDTRDVLGM
CLEISGTKGS SSTLIREKCT LCPRGLLDST RAHDYHQTLN LMLKCNGLRS SSSKMFICEH
TRGMDLDAKE RRLEQLEDDN LESSNWAFWV EVGYLSNLSR AVRNPGVPQI SSRGGIQRSP
AFYSTGVEFQ SPYNMAGSKT VRIVEVGPRD GLQNVKTVVD TSTKLELIQR LRGAGLQNIE
ITSVVSPKAI PQLADCRKIL SAPNVKRWQQ TDTTLRLPVL VPNTKGLHIA LEHGVREVAV
FVSATEGFSR ANINCTVDES LERAKQVATE ARTAGVLVRG YVSCIFADPF DGPTPLTAVS
RAVRSLLDMG CYEVSLGDTL GIGTPSDVRR LLEYLKSQNI HTEKLAGHFH DTYGQALANV
WTAYECGLRT FDSSVGGLGG CPFAPGAKGN VATEDVVYLF QQAGVDTGVD LQQVVDIGVW
ISHALAKPND SRAGAALASK SKRSSTGSSS KFTSRPKEAW EWSVLEQSDN IVAQRAGANG
NIVLNKPQNG NTLTFPMISE IIRTFKSFEN DPSISRILIS ANGKFFCTGM DLSQAAQAVG
RGGDASAKLF QALTDLFELI DNSPKVTIAC IQGSAFGGGI GLAFACDIRI SISSATFTLS
EAKLGMCPAV ISKYVIREWG FGLSREAMLT ARSLTASELK SAGAISMVAE TPSELDIKTK
TLLAQLRHSS PGGSSMSKEL VKLSWRHAGM PEQRDGIFRL FKSMMEPGSD AVHGIAEFQQ
KRKVDWDSLN QVPRAKI
//
