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
//