ID   G7TDT9_XANOB            Unreviewed;       896 AA.
AC   G7TDT9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595,
GN   ECO:0000313|EMBL:AEQ95078.1};
GN   ORFNames=XOC_0872 {ECO:0000313|EMBL:AEQ95078.1};
OS   Xanthomonas oryzae pv. oryzicola (strain BLS256).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=383407 {ECO:0000313|EMBL:AEQ95078.1, ECO:0000313|Proteomes:UP000008851};
RN   [1] {ECO:0000313|EMBL:AEQ95078.1, ECO:0000313|Proteomes:UP000008851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BLS256 {ECO:0000313|EMBL:AEQ95078.1,
RC   ECO:0000313|Proteomes:UP000008851};
RX   PubMed=21784931; DOI=10.1128/JB.05262-11;
RA   Bogdanove A.J., Koebnik R., Lu H., Furutani A., Angiuoli S.V., Patil P.B.,
RA   Van Sluys M.A., Ryan R.P., Meyer D.F., Han S.W., Aparna G., Rajaram M.,
RA   Delcher A.L., Phillippy A.M., Puiu D., Schatz M.C., Shumway M.,
RA   Sommer D.D., Trapnell C., Benahmed F., Dimitrov G., Madupu R., Radune D.,
RA   Sullivan S., Jha G., Ishihara H., Lee S.W., Pandey A., Sharma V.,
RA   Sriariyanun M., Szurek B., Vera-Cruz C.M., Dorman K.S., Ronald P.C.,
RA   Verdier V., Dow J.M., Sonti R.V., Tsuge S., Brendel V.P., Rabinowicz P.D.,
RA   Leach J.E., White F.F., Salzberg S.L.;
RT   "Two new complete genome sequences offer insight into host and tissue
RT   specificity of plant pathogenic Xanthomonas spp.";
RL   J. Bacteriol. 193:5450-5464(2011).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
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DR   EMBL; CP003057; AEQ95078.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7TDT9; -.
DR   KEGG; xor:XOC_0872; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   Proteomes; UP000008851; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; 1.
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, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:AEQ95078.1}.
FT   REGION          44..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        143
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        562
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   896 AA;  99321 MW;  8A2ED252776F38A3 CRC64;
     MFATPDLPLR DDVRRLGALV GDLLAEQVSA EFLDEIERVR TTAISRRESD APPSTLSEQL
     TGREPRDAEA LVRAFSTYFQ VVNIAERVHR IRRRREYQRS GTDTPQPDGL HDALRRLKAQ
     GVTLDELSQW LPRIDVEPVF TAHPTEAVRR ALLEKEQLMV ASLVDNLDGM RTPNERTSDA
     ARFRMALTAS WQTADSSPVR PTVGDEREHV GFYLTQVLYR VIPVMYETLE HAIEETYGSV
     PALPRLLRFG TWVGGDMDGN PNVDANTIAG TLDAQRRAVL DRYQKELWQL ASLLSQSTTL
     VQVSPELMTQ LERYRALLPD AAARSRPRHG DMPYRLLNDL MRARLQATLD DADGAYTAPS
     ELEDDLQLIL DSLQANKGLH AGWFAVRRLL WRVRSFGFHL ARLDVRQESS VHARAVADAL
     GQTDWDGQDA TRRAAVLGPY ACGQEALPRA QDEGNARLDA VFAALADART RHGADALGSY
     IISMAHNRAD VLTVLALARR GGLVDAAGTV PLDIVPLFET VDDLRGGTGT VQDLLADPVY
     RQHLAARGDT QMVMLGYSDS GKDGGIAASR WGLQRAQVEL LEAAADLGVR LTFFHGRGGS
     IARGGGKTSR ALDAAPRGSV DGRLRVTEQG EVIHRKYGIR ALALRSLEQM TGAVLLSSLR
     PRAPEPREAR WRPVMDLVAE RSTVAYRAFV AAPEFMQYFR LATPIDVIER MTLGSRPSRR
     LGQDAALSNL RAIPWVFAWS QARAVIPGWY GVGSGLQAAV DAGHEDTLRE MAQDWPFFRT
     FLDDVAMVLS KGDLNIAELF SRLSGDLHTR FFPLIRDELA LTKGWVKALL QQQSLLQHDP
     RLALSIRLRN PYIDPISVLQ VDLLQRWRAT DGEDEALLRA LVACVNGVSQ GLQNTG
//