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Database: UniProt
Entry: F6HQA2_VITVI
LinkDB: F6HQA2_VITVI
Original site: F6HQA2_VITVI 
ID   F6HQA2_VITVI            Unreviewed;       570 AA.
AC   F6HQA2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
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   OrderedLocusNames=VIT_03s0063g00290 {ECO:0000313|EMBL:CCB56859.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB56859.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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; FN596006; CCB56859.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6HQA2; -.
DR   STRING; 29760.F6HQA2; -.
DR   PaxDb; 29760-VIT_03s0063g00290-t01; -.
DR   EnsemblPlants; Vitvi03g00513_t001; Vitvi03g00513_P001; Vitvi03g00513.
DR   Gramene; Vitvi03g00513_t001; Vitvi03g00513_P001; Vitvi03g00513.
DR   eggNOG; KOG0540; Eukaryota.
DR   HOGENOM; CLU_018822_0_1_1; -.
DR   InParanoid; F6HQA2; -.
DR   UniPathway; UPA00363; UER00861.
DR   Proteomes; UP000009183; Chromosome 3.
DR   ExpressionAtlas; F6HQA2; baseline and differential.
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:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   DOMAIN          50..306
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          312..570
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   570 AA;  61851 MW;  AAF8EBEC9F3076F7 CRC64;
     MLRVLGRRAS TSHQWRNPVS LLQKCQFCIG VLPDGVDRQS PSFSQNSAIM NDYISELKSH
     VQKVLGGGGA ESVRRNRSRN KLLPRERIDR LLDPGSSFLE LSQLAGHELY EEPLPSAGII
     TGIGPVHGRL CMFVANDPTV KGGTYYPITV KKHLRAQEIA AQCKLPCIYL VDSGGAYLPK
     QADVFPDRDN FGRIFYNEAQ MSAEGIPQIA LVLGSCTAGG AYIPAMADES VMVKGNGTIF
     LAGPPLVKAA TGEEVSAEDL GGATVHCKTS GVSDYFAQDE LHGLAIGRNI IKNFHMAGKL
     GIVNELQNII PEFKEPVYDV KELRSIAPAD HKQSFDIRSV IARIVDGSEF DEFKKLYGTT
     LVTGFARIFG QPVGIIGNNG ILFNESALKG AHFIEICTQR NIPLVFLQNI TGFMVGSRSE
     ANGIAKSGAK MVMAVSCAKV PKITIIVGGS FGAGNYAMCG RAYSPNFMFL WPNARISVMG
     GAQAAGVLSQ IERGNKKKQG IQWPKDEEEA FKAKVVEAYE KEGSSYYSTA RLWDDGIIDP
     ADTRKIIGLC ISATTTNHAP EDTKYGVFRM
//
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