GenomeNet

Database: UniProt
Entry: V7C1X2_PHAVU
LinkDB: V7C1X2_PHAVU
Original site: V7C1X2_PHAVU 
ID   V7C1X2_PHAVU            Unreviewed;       276 AA.
AC   V7C1X2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Biotin carboxyl carrier protein of acetyl-CoA carboxylase {ECO:0000256|RuleBase:RU364072};
GN   ORFNames=PHAVU_004G034300g {ECO:0000313|EMBL:ESW23290.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW23290.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000256|ARBA:ARBA00003761, ECO:0000256|RuleBase:RU364072}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU364072}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU364072}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM002291; ESW23290.1; -; Genomic_DNA.
DR   RefSeq; XP_007151296.1; XM_007151234.1.
DR   AlphaFoldDB; V7C1X2; -.
DR   STRING; 3885.V7C1X2; -.
DR   EnsemblPlants; ESW23290; ESW23290; PHAVU_004G034300g.
DR   GeneID; 18631900; -.
DR   Gramene; ESW23290; ESW23290; PHAVU_004G034300g.
DR   KEGG; pvu:PHAVU_004G034300g; -.
DR   eggNOG; ENOG502QUI2; Eukaryota.
DR   OMA; RIQCANR; -.
DR   OrthoDB; 3640642at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000226; Chromosome 4.
DR   GO; GO:0009317; C:acetyl-CoA carboxylase complex; IEA:InterPro.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   InterPro; IPR001249; AcCoA_biotinCC.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR00531; BCCP; 1.
DR   PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   PRINTS; PR01071; ACOABIOTINCC.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   4: Predicted;
KW   Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|RuleBase:RU364072};
KW   Chloroplast {ECO:0000256|RuleBase:RU364072};
KW   Fatty acid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364072};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364072};
KW   Plastid {ECO:0000256|RuleBase:RU364072};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT   DOMAIN          199..275
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          71..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   276 AA;  29097 MW;  99FD71C05511D5D0 CRC64;
     MASFSVPCPK CPSTSSPSFG FKSQQLPFQT GFSFKPFPSF RSLFAESASS RIQCPDRKQF
     PVLKAAKVEN SNSNSAPATV KGPNVASSKE KEVLNGKHSG STTADQASVT AFLSQVSNLI
     KLVDSKDIVE LQLEQSDCEL LIRKKEALQP PPAPASPPPM HYATFPPAAA APAAAPASSS
     PPKALPALPS PGKASSSSHP PQKSPIAGTF YRSPGPGEPP FVKVGDKVKK GQVICIIEAM
     KMMNEIEADQ SGTITEILIE DAKPISLDTP LFVIVP
//
DBGET integrated database retrieval system