ID   CAPP_PSYIN              Reviewed;         878 AA.
AC   A1SRH8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=Ping_0226;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; CP000510; ABM02093.1; -; Genomic_DNA.
DR   RefSeq; WP_011768652.1; NC_008709.1.
DR   AlphaFoldDB; A1SRH8; -.
DR   SMR; A1SRH8; -.
DR   STRING; 357804.Ping_0226; -.
DR   EnsemblBacteria; ABM02093; ABM02093; Ping_0226.
DR   KEGG; pin:Ping_0226; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000000639; 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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..878
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025582"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   878 AA;  98945 MW;  59D1507D8EF34D40 CRC64;
     MTEEYSNLRS NVSLLGQLLG KSIGGHLGEE FLDKIETIRQ LSKSSRAGNQ QDGVALIDML
     THLSDDELVP VARAFTHFLN LANIAEQFHG ISRHCDSGVC APEPIKDLIS KFKNSNLSQQ
     EMQQSVNELK MEMVLTAHPT EITRRTLIHK HIAINDCLSY LEISDISDKE RDLLLNRLEQ
     LITQAWHTND IRQKRPTPVD EAKWGFATIE KSLWQAVPQF IRDLESELQS GLGLSLPLEA
     SPITFTSWMG GDRDGNPFVT AKVTQEVLLS SRWVAVSLYL KDISQLTDEL SMDNCDPALR
     SVVGDNAAEP YRAILRKLRS ELKETLASLS ATLQNQRSDE KDIITTSKQL KEPLLLCYHS
     LKNMGMNSIA NGLILDILRR LNCFGINLLK LDIRQDAERH GNTLSELTRY LGIGDYNAWN
     EEDKQAFLLQ ELNNKRPLFP SQWNPSAEVQ EVLDTCKVVA QTDPEALGIY IISMARQASD
     VLAVQLILKE VGCPFRIPVA PLFETLDDLN NSAAVMKRLF AIDWYRGYIN GIQHVMIGYS
     DSAKDAGVIA ANWAQYTSQE ALVKLSAEND INLVLFHGRG GTIGRGGAPA RQALLSQPPG
     SLKGGLRVTE QGEMIRFKFG LPKVAVQSLN QYAAAVLEAN LLPPPAPKQE WRDVMQQFSD
     QSCQEYRHFV REEPDFVPYF RSVTPEVELG KLALGSRPSK RKPSGGIESL RAIPWIFAWS
     QNRLMLPAWL GAGTSLKTLL NEGKKPLLQE MYQHWPFFHT RLEMFEMVFL KADEELTKFY
     EERLVPKELW PLGQRLRDNL TLTRETVLET IPDHQLMQEQ PWIKESISLR NPYVDPLNML
     QAELLYRSRE NGDEICPVVD QALMVTIAGI AAGLRNTG