ID V7C5B2_PHAVU Unreviewed; 1055 AA.
AC V7C5B2;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN ORFNames=PHAVU_003G024800g {ECO:0000313|EMBL:ESW25309.1};
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:ESW25309.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001071};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346}.
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DR EMBL; CM002290; ESW25309.1; -; Genomic_DNA.
DR RefSeq; XP_007153315.1; XM_007153253.1.
DR AlphaFoldDB; V7C5B2; -.
DR STRING; 3885.V7C5B2; -.
DR EnsemblPlants; ESW25309; ESW25309; PHAVU_003G024800g.
DR GeneID; 18633669; -.
DR Gramene; ESW25309; ESW25309; PHAVU_003G024800g.
DR KEGG; pvu:PHAVU_003G024800g; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR OMA; TKHYDEQ; -.
DR OrthoDB; 355614at2759; -.
DR Proteomes; UP000000226; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 2.
DR HAMAP; MF_00595; PEPcase_type1; 1.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR022805; PEP_COase_bac/pln-type.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR033129; PEPCASE_His_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR Pfam; PF00311; PEPcase; 2.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 3: Inferred from homology;
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT REGION 342..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 722
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1055 AA; 118094 MW; CE3CECDBF99EFFE0 CRC64;
MTDITDDIAE EISFQDFDDD CNMLGSLLND ILQREAGPIF VDKLEKIRVL AQSACNMRHA
GIEDMAELLE KQLASELSKM TLEEALTLAR AFSHHLTLMG IAETHHRVRK GGNRALIAKS
CDDIFNQLLQ DGVTPDELYN SVCKQEVEIV LTAHPTQINR RTLQYKHIKI AHLLDYNDRP
DLGHEDRDML IEDLVREITS IWQTDELRRE KPTPVDEARA GLNIVEQSLW KAVPHYLRRV
SSALRKHTGK PLPLTCTPIK FGSWMGGDRD GNPNVTAKVS KDVSLLSRWM AIDLYVREVD
SLKFELSMKR CSDKLSKLAQ EILEEANDEE NHRELWNESR SVSQMKYSSK QGSPLPTKLP
SGAHLPSCAE KGGSEHPRLM PGADYKQFNP KGGEISSSTE SSGGSPNVRS SVPISPNSSA
SSLVSMTRSP SFNSSQQLLA QRKLFAESQT GRTSFHRLLE PKLPQLPGIA PYRVVLGNVK
DKLLRTRRRL ELLLEDGPCE HNPTNYYETT DQLLEPLLLC YESLQSCGSG VLADGRLADL
IRRVTTFGMV LMKLDLRQES GRHAETLDAV TRYLDLGTYS EWDEEKKLNF LTRELKGKRP
LIPPSIEVVP DVREVLDTFR TAAELGSDSF GAYVISMASN ASDVLAVELL QKDARLAVSG
ELGRACPGGT LRVVPLFETV KDLRGAGSVI RKLLSIDWYR QHILKNHNGH QEVMVGYSDS
GKDAGRFTAA WELYKAQEDV VAACKEYGIK VTLFHGRGGS IGRGGGPTYM AIQSQPPGSV
MGTLRTTEQG EMVQAKFGLP QTAVRQLEIY TTAVLLATLR PPLPPREEKW RNMMEDISNI
SCKCYRSVVY ENPEFLSYFH EATPQSELGF LNIGSRPTRR KSTTGIGHLR AIPWVFAWTQ
TRFVLPAWLG VGAGLKGASE KGQTEELRAM YKEWPFFQST IDLIEMVLGK ADIPIAKHYD
EVLVSEKRQK LGSQLREELI QTGKFVLSVS GHEKPQQNNR SLRKLIESRL PFLNPMNMLQ
VEILKRLRSD DDNLKARDAL LITINGIAAG MRNTG
//
