ID   I0EMK4_HELC0            Unreviewed;       870 AA.
AC   I0EMK4;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419};
GN   OrderedLocusNames=HCW_04530 {ECO:0000313|EMBL:AFI04173.1};
OS   Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=182217 {ECO:0000313|EMBL:AFI04173.1, ECO:0000313|Proteomes:UP000005010};
RN   [1] {ECO:0000313|Proteomes:UP000005010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-429 / MIT 00-7128 {ECO:0000313|Proteomes:UP000005010};
RA   Kersulyte D., Berg D.E.;
RT   "Complete genome sequence of Helicobacter cetorum strain MIT 00-7128.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670}.
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};
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DR   EMBL; CP003479; AFI04173.1; -; Genomic_DNA.
DR   RefSeq; WP_014661043.1; NC_017737.1.
DR   AlphaFoldDB; I0EMK4; -.
DR   STRING; 182217.HCW_04530; -.
DR   KEGG; hce:HCW_04530; -.
DR   PATRIC; fig|182217.3.peg.967; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_7; -.
DR   Proteomes; UP000005010; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:InterPro.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   InterPro; IPR021135; PEP_COase.
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   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Pyruvate {ECO:0000313|EMBL:AFI04173.1}.
FT   ACT_SITE        119
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        537
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   870 AA;  100176 MW;  9DC180914244D0A6 CRC64;
     MKKSPHFLQE LVLIKRLFLQ MLKECQEEEM ANLFLSLCHA FEKNSFKKSH KILQEIIASQ
     QLLGIIKVFS LYNILINIVE ERHKINSTSY SFKENQKPLS QKAKNALKHL AFYPVFTAHP
     TQSMRRTFLE AYQEISTYVA CLSNNPTQTI QEKSEQEIKY RLHLLYKSHL ARQEKLEVLS
     ELDNLLYLVE TSILPSALKT LNSIQKALNE PLKQSPIILG SWIGGDRDGN PFVTNALMTQ
     TLRIQHAFII ELYIKEVRAL TRELSLSSDF CTISDTFKQS IEQEKMHLDP SDAILHQHEP
     FRAKLLLMEK KLKNRLLSVN SPLEIPYTYH NIEEFIHDID LMLNHLEPYL RPHLERLRHL
     ALLAGFHALR LDFREHKEVF LNALSETFSF LGLADSDFLS KNETKKLEII NNAFLYLEKN
     PLDLHSLIEH ISLKSANILE AFSKIAWAKQ NISKESVRSV IISMSESASD ILGVLWLVQL
     AKLENEISLT PLFETIDDLE NAPKIMQTLS QNPHYNNYLN HQNRNQQIMI GYSDSSKDGG
     IFASNYYLNN AITKLIELEK SLNLSFLLFH GRGGSVSRGG LSLESALDCA PYKSAKNILK
     LTEQGEVISL KYLNLENAEY NLHNALNALL KKNLQEKAQK TSKEHEEILQ TIARLSYQAY
     RKLVYETKGF LEYFKLATPI YFIQELPLGS RPSKRKDSTK IEDLRAIPWV FAWTQNRCIL
     PAWYGLGSAL KTLEPTILQT LYKENKLFKV VLDNVAQVLL KVDLEIFESY HSLAKDLFNA
     KEIFNAICDE FKITKELILC ARKESELLES EPTTYYSILF RRPYLNALNA LQIELIKAFY
     ATKDKDKQAH LLHQVHSSIV GIAQGMRNTG
//