ID H3G9Y1_PHYRM Unreviewed; 563 AA.
AC H3G9Y1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-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};
OS Phytophthora ramorum (Sudden oak death agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=164328 {ECO:0000313|EnsemblProtists:Phyra71891, ECO:0000313|Proteomes:UP000005238};
RN [1] {ECO:0000313|Proteomes:UP000005238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pr102 {ECO:0000313|Proteomes:UP000005238};
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2] {ECO:0000313|EnsemblProtists:Phyra71891}
RP IDENTIFICATION.
RC STRAIN=Pr102 {ECO:0000313|EnsemblProtists:Phyra71891};
RG EnsemblProtists;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR EMBL; DS566055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3G9Y1; -.
DR STRING; 164328.H3G9Y1; -.
DR EnsemblProtists; Phyra71891; Phyra71891; Phyra71891.
DR VEuPathDB; FungiDB:PSURA_71891; -.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; H3G9Y1; -.
DR OMA; AYLPIMS; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000005238; Unassembled WGS sequence.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
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:UP000005238}.
FT DOMAIN 50..306
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 306..555
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 563 AA; 60776 MW; E2579167723C2ECF CRC64;
MLRNVYGSVL GAPARRSLLL SAGVLDSFSN VLDGALNVKS AQFQESLAHM AKLTSELRER
VAHARQGGGE AARARHESRG KMPVRDRIDS LLDPGSPFLE LSPLAAYDMY GGGVPSAGIV
TGVGRINGVE CMILGNDATV KGGTYFPLTV KKHLRAQEIA QENRLPCVYL VDSGGAFLPL
QADIFPDREH FGREFYNQAT MSAMGIPQIA VVMGSCTAGG AYVPAMSDES VIVKGNGTVF
LGGPPLVKAA TGEVVTPEEL GGADVHCRTS GVTDHYANND AHALDITRRI VSNLNYRKQP
AVTQTPIEEP LYSPDELGGV IPVDSRKPFD VRKVIARIVD GSRFDEFKKE YGSTIVTGFA
RLYGNPVGIV ANNGILFSES SVKAAHFIEL CSQRGIPLLF LQNITGFMVG KKAEHGGIAK
DGAKMVMAVS NAKVPKLTCI IGGSYGAGNY GMCGRAFSPR FLYMWPNARI SVMGGEQAAG
VLAQVQRDNY ERRKESWSAE EEAAFKQPIL DKYEHESSAY YSTARLWDDG IIDPKDTRKV
LGLSLSAALN EEPKETKFGV FRM
//
