ID J3KVR9_ORYBR Unreviewed; 1035 AA.
AC J3KVR9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN Name=102711100 {ECO:0000313|EnsemblPlants:OB01G10750.1};
OS Oryza brachyantha (malo sina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB01G10750.1};
RN [1] {ECO:0000313|EnsemblPlants:OB01G10750.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB01G10750.1};
RX PubMed=23481403;
RA Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA Chen M.;
RT "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT Oryza genome evolution.";
RL Nat. Commun. 4:1595-1595(2013).
RN [2] {ECO:0000313|EnsemblPlants:OB01G10750.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2013) to UniProtKB.
CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003774}.
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 -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008346}.
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DR RefSeq; XP_006643661.1; XM_006643598.2.
DR AlphaFoldDB; J3KVR9; -.
DR STRING; 4533.J3KVR9; -.
DR EnsemblPlants; OB01G10750.1; OB01G10750.1; OB01G10750.
DR GeneID; 102711100; -.
DR Gramene; OB01G10750.1; OB01G10750.1; OB01G10750.
DR KEGG; obr:102711100; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_2_0_1; -.
DR OMA; FGWTQSR; -.
DR OrthoDB; 355614at2759; -.
DR Proteomes; UP000006038; Chromosome 1.
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 Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT REGION 329..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..419
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 701
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1035 AA; 116062 MW; 82700C87C255B672 CRC64;
MTDTTDDIAE GISFQAFEDD CRLLGSLLHD VLLRELGPRF IHLLERITIL AQSAVNMRAA
GMEDTAAVVE KQLWADLSAM SLEDSLSLSR AFSHHLNLMS IADTYHRVRK ARNFSDLSKS
CDDTFDKLIQ SGVPPEELYD TVCKQEVEIV LTAHPTQINR RTLQYKHLRI AHLLEFNDRA
DLSHEDKEIL IEDLVREITA IWQTDELRRH KPTPVDEARA GLHIVEQSLW KAIPHYLRRV
SNALKKHTGK PLPLTCTPIK FGSWMGGDRD GNPNVTAKVT RDVSVLSQWM AIDLYIRELD
TLSFELSIKK CSEKLENLAN DILLKESASE DQKTNTWKQT GRQSNLKPQP SLPLPAQLPS
GADLPSCTEC NDGESQIRMS KLPGNPKHKL FLNTTEKRED STLPSPSHRQ MGRTPSGGQL
RKMFTESQMG RSSFRKLLEP GISDRPGITP YRVVLGDVKE KLMNTRKRFE LLLEDVPCDR
DTSEYYETSD QLLEPLLLCY QSLQSCGSSV LADGRLADLI RRVATFGMVL MKLDVRQESG
RHTETLDAVT SYLDLGVYSE WDEEKKLDFL TRELKGKRPL VPPYIQVTAD VQEVLDTFRV
AAELGSDALG AYVISMASNA SDVLAVELLQ KDARLTVSGD LGRPCPGGTL RVVPLFETVK
DLREAGSAIR KLLSIDWYRE HIIKNHNGHQ EVMVGYSDSG KDAGRFTAAW ELYKAQEDVV
AACNEFGIKV TLFHGRGGSI GRGGGPTHLA IQSQPPGSVM GTLRSTEQGE MVQAKFGLPQ
TSVRQLEIYT TAVLLATLRP PQPPRDPNWR RVMEEISRVS CAQYRSTVYE NPEFIKYFQE
ATPQAELGYL NIGSRPAKRR ATAGISNLRA IPWVFAWTQT RLVLPAWLGV GRGLQDACDK
GHADELRAMY EEWPFFQSTV DLIEMVVAKA DAPMAKHYDD VLVGDGGRRA LGAELRQELA
RTESCVLAVS GHKKLSANNR SLRKLIESRL TYLNPINMLQ VEVLRRLRQD HDNRKLRDAL
LITINGIAAG MRNTG
//
