ID A0A0F2MB03_SPOSC Unreviewed; 615 AA.
AC A0A0F2MB03;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SPSK_08853 {ECO:0000313|EMBL:KJR85351.1};
OS Sporothrix schenckii 1099-18.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1397361 {ECO:0000313|EMBL:KJR85351.1, ECO:0000313|Proteomes:UP000033710};
RN [1] {ECO:0000313|EMBL:KJR85351.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR85351.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25351875; DOI=10.1186/1471-2164-15-943;
RA Teixeira M.M., de Almeida L.G., Kubitschek-Barreira P., Alves F.L.,
RA Kioshima E.S., Abadio A.K., Fernandes L., Derengowski L.S., Ferreira K.S.,
RA Souza R.C., Ruiz J.C., de Andrade N.C., Paes H.C., Nicola A.M.,
RA Albuquerque P., Gerber A.L., Martins V.P., Peconick L.D., Neto A.V.,
RA Chaucanez C.B., Silva P.A., Cunha O.L., de Oliveira F.F., dos Santos T.C.,
RA Barros A.L., Soares M.A., de Oliveira L.M., Marini M.M.,
RA Villalobos-Duno H., Cunha M.M., de Hoog S., da Silveira J.F., Henrissat B.,
RA Nino-Vega G.A., Cisalpino P.S., Mora-Montes H.M., Almeida S.R.,
RA Stajich J.E., Lopes-Bezerra L.M., Vasconcelos A.T., Felipe M.S.;
RT "Comparative genomics of the major fungal agents of human and animal
RT Sporotrichosis: Sporothrix schenckii and Sporothrix brasiliensis.";
RL BMC Genomics 15:943-943(2014).
RN [2] {ECO:0000313|EMBL:KJR85351.1, ECO:0000313|Proteomes:UP000033710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1099-18 {ECO:0000313|EMBL:KJR85351.1,
RC ECO:0000313|Proteomes:UP000033710};
RX PubMed=25480940;
RA Teixeira Mde M., Rodrigues A.M., Tsui C.K., de Almeida L.G.,
RA Van Diepeningen A.D., van den Ende B.G., Fernandes G.F., Kano R.,
RA Hamelin R.C., Lopes-Bezerra L.M., Vasconcelos A.T., de Hoog S.,
RA de Camargo Z.P., Felipe M.S.;
RT "Asexual propagation of a virulent clone complex in a human and feline
RT outbreak of sporotrichosis.";
RL Eukaryot. Cell 14:158-169(2015).
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:KJR85351.1}.
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DR EMBL; AXCR01000007; KJR85351.1; -; Genomic_DNA.
DR RefSeq; XP_016588027.1; XM_016735439.1.
DR AlphaFoldDB; A0A0F2MB03; -.
DR GeneID; 27670716; -.
DR KEGG; ssck:SPSK_08853; -.
DR VEuPathDB; FungiDB:SPSK_08853; -.
DR OrthoDB; 5474505at2759; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000033710; 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;
FT DOMAIN 101..363
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 378..608
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 615 AA; 65373 MW; 7940917E9C620A6F CRC64;
MTFSRNARGA LRLTPQLCNT CRRTTATTAP AATAARALST QLSPVRPVQR SLARTTNAPV
VPSSRGIAAF AAAGPSDATL SRIPSTVDTT SDIYQENLGL MKEAMERLDR LTRAAQRGGS
EKARAKHVGR GKMLPRDRVA ALVDPGTSFM ELSTLAGENL YEEDGGKPLA LPSGGIITGI
GVVEGVTCMI VANDSTVKGG TYYPITIKKH LRAQEIAAQN RLPCLYLVDS GGANLPHQAD
VFPDRDHFGR IFYNQARMSA QGIPQLAVVM GPCTAGGAYV PAMSDESIIV QNQGHIFLAG
PPLVKAATGE EVTPEELGGG LMHSSVSGVT DYLAVDDAHA IALARRSVAN LNYPQQTPSL
EKTTAAGAAA TFAEPVSDPE ELLGIASTNL RRPISAHEVI SRIVDGSAFA EFKKDYGTTL
VTGFARIYGQ RVGIVANNGV LLSTAAVKGA HFIELCSQRG IPLVFLQNIS GFMVGKEAER
EGIAKHGAKL VNAVACADVP KLTVVVGGSY GAGNYGMCGR AYSPRFLWMW PNARIAVMGS
EQLATVMETV GRADPELRNR IERESDAVYS SARLWDDGII PPQHTRRYLG LGLRAAMGGR
NEVEPNATKF GVFRM
//
