ID A0A0F4G8F9_9PEZI Unreviewed; 566 AA.
AC A0A0F4G8F9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=TI39_contig4339g00006 {ECO:0000313|EMBL:KJX93302.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX93302.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJX93302.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJX93302.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-2015) 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:KJX93302.1}.
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DR EMBL; LAFY01004298; KJX93302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4G8F9; -.
DR STRING; 1047168.A0A0F4G8F9; -.
DR OrthoDB; 5474505at2759; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000033647; 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:UP000033647}.
FT DOMAIN 65..322
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 323..561
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 566 AA; 60534 MW; 4EEA1EA00FFC8C72 CRC64;
MASLLPSRAF ARALHHIPRR RMTAPTQCRR TAATYSSPQQ ANQPSIIQTT VDTQSNGYKE
NAAAMAEYTA RLAELHATAA KGGSEKSRKK HVERGKMLVR DRITALIDPG TSFIELSALA
AHDMYPGEDV PAAGIVSGIG TVEGVQCVIL ANDSTVKGGS YYPMTIKKHL RAQEIAQQNR
LPCIYLVDSG GANLPNQADV FPDRDHFGRM FFNQANMSAM GIPQISVVMG SCTAGGAYIP
SMSDESIIVA EQGTIFLAGP PLVKAATGEE VTAEELGGGK LHSEVSGVTD YLAVDDAHAL
VLARRSISNL NYPTTPNPSR KQAWKEPLYD IEELGGIVGT NLKQSINMHD VIARIVDGSE
FSEFKPSYGT SLLTGFATIH GHPVGIIANN GILFSESSLK GAHFIQLCCQ RNIPLIFLQN
ISGFMVGQDA EKGGIAKNGA KLVTAVACAS VPKFTVLVGS SAGAGNYGMC GRAYSPRFLW
SWPSAKTSVM GAEQLTNVMA AVGKKVDPEL KARIERESEV TFGTARLWDD GVIPPSHTRR
VLGMGLDAAM TGSVETKETK FGVFRM
//
