ID G9MQ30_HYPVG Unreviewed; 572 AA.
AC G9MQ30;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-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:carbon dioxide ligase subunit beta {ECO:0000256|ARBA:ARBA00031237};
GN ORFNames=TRIVIDRAFT_76806 {ECO:0000313|EMBL:EHK23979.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK23979.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK23979.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK23979.1}.
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DR EMBL; ABDF02000005; EHK23979.1; -; Genomic_DNA.
DR RefSeq; XP_013958180.1; XM_014102705.1.
DR AlphaFoldDB; G9MQ30; -.
DR STRING; 413071.G9MQ30; -.
DR EnsemblFungi; EHK23979; EHK23979; TRIVIDRAFT_76806.
DR GeneID; 25797858; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_76806; -.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; G9MQ30; -.
DR OMA; AYLPIMS; -.
DR OrthoDB; 5474505at2759; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000007115; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 67..324
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 334..565
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT COILED 46..80
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 572 AA; 61303 MW; F36038A31F115189 CRC64;
MSLSRPCRQA LRLSHALRPS IKASPSSQLL RRSAATLTPP HQAAAISRLQ TNVDASSEEF
KENERQMAEV TARLQELTTT IQKGGSQKAR DKHIARNKML PRDRVAALID PGTTFLELSP
MAGHELYPEA EVPAGGIITG VGVVEGVTCV IVANDSTVKG GTYYPITVKK HLRAQAVAQE
NKLPCIYLVD SGGANLPHQA DVFPDQNHFG RIFYNQARMS SQGIPQISVV MGPCTAGGAY
VPAMSDESII VQEQGHIFLA GPPLVKAATG EVVSHEDLGG GKMHSSVSGV TDYLAVDDAH
AITLARRSIS NLNWPARSAS TQPPAATYAE PLYDPNELMG IATTNLRKPM PIREIIARIV
DGSEFAEFKR DFGTTLVTGF ASIYGQKVGI VANDGILFAS SSVKGAHFIE LCAQRGIPLV
FLQNISGFMV GSASERDGIA KHGAKLVTAV ACADVPKFTV VVGGSYGAGN YGMCGRAYSP
RFLWMWPNAR VGVMGSEQLT SVMETVGKAA DPELKARIER ESEATYSSAR LWDDGIIPPQ
HTRQYLGLGL RAAMGGRNEV KAGDTKFGVF RM
//
