ID A0A1S3V119_VIGRR Unreviewed; 1036 AA.
AC A0A1S3V119;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN Name=LOC106770762 {ECO:0000313|RefSeq:XP_014512041.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014512041.1};
RN [1] {ECO:0000313|RefSeq:XP_014512041.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014512041.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_014512041.1; XM_014656555.2.
DR AlphaFoldDB; A0A1S3V119; -.
DR STRING; 3916.A0A1S3V119; -.
DR GeneID; 106770762; -.
DR KEGG; vra:106770762; -.
DR OrthoDB; 355614at2759; -.
DR Proteomes; UP000087766; Chromosome 8.
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:UP000087766}.
FT REGION 330..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..423
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 703
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1036 AA; 115769 MW; C59FDAB9B4A20766 CRC64;
MTDITDDVAE EISFQSFDDD CRLLGNLLND ILQREVGTNL VDKIERIRVL AQSGCNMRQA
GILNMAELLE KQLASELSKM TLEEAFTLAR AFSHYLTLMG IAETHHRVRK GGNVAQTAKS
CDDIFNQLVQ GGVSPEELYD TVCKQEVEIV LTAHPTQINR RTLQFKHVRI AHLLDYNDRP
DLSIEDREMV IEDLVREITS IWQTDELRRQ KPTPVDEARA GFNIVDQSLW KAVPHYLRRV
SNALKKHTGK PLPLTCTPIK FGSWMGGDRD GNPNVTAKVT KDVSLLSRWM AIDLYIREVD
SLRFELSMNQ CSDRLSRLAH DILEAKRDNP RENWNQSVNR SPALPTQLPA RAHLPSIAEN
GESRHPRLDI PGPDHMQSNH KDGGAALSSS TSKNPNPNIQ SQGSSSANSN ASSAPTSSSF
GQKKLYAEPQ TGKSTFQKLL EPMLPQLPGI APYRIVLGNV KDKLERSRRR LELLLEDVAC
DYDSSEYYET SDQLLEPLLL CYESLQSCGS GVLADGRLAD LIRRVATFGM VLMKLDLRQE
SGRHAEALDA ITEYLDMGTY SEWDEEKKLD FLTKELKGKR PLVPLSIEVP SDVKEVLDTF
RIAAELGSDS LGAYVISMAS NASDVLAVEL LQKDARLAAI GESGKACPGG TLRVVPLFET
VKDLRGAGAV IRKLLSIDWY REHIIKNHNG HQEVMVGYSD SGKDAGRFTA AWELFKAQED
VVAACNDYGI KVTLFHGRGG SIGRGGGPTY LAIQSQPPGS VMGTLRSTEQ GEMVEAKFGL
PQIAVRQLEI YTTAVLLATL RPPIPPREEK WRNVMEEISN ISCQCYRNVV YENPEFLAYF
HEATPEAELG FLNIGSRPAR RKSSRGIGHL RAIPWLFAWT QTRFVLPAWL GVGAGLKGAC
EKGLTEDLKA MYKEWPFFQS TIDLIEMVLG KADIPIAKHY DEVLVSQERQ ELGGELRSEL
MTAEKFVLVI SGHEKLQQNN RSLRRLIENR LPFLNPLNML QVEILKRLRR DDDNIKIRDA
LLITINGIAA GMKNTG
//