ID   CAPP_SHELP              Reviewed;         878 AA.
AC   A3Q9C4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=Shew_0200;
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-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; CP000606; ABO22072.1; -; Genomic_DNA.
DR   RefSeq; WP_011864007.1; NC_009092.1.
DR   AlphaFoldDB; A3Q9C4; -.
DR   SMR; A3Q9C4; -.
DR   STRING; 323850.Shew_0200; -.
DR   KEGG; slo:Shew_0200; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001558; 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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..878
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025587"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   878 AA;  98940 MW;  202CEAAE56830783 CRC64;
     MTDMYASLRS NVGTLGQILG DTIRTHMDEP FLDKIEQIRH LAKSSRQGND TAREQMLTLL
     AALPDEELVP FAKAFNQFLN LANIAEQFHT ISRNCDELVC VPDPVDQLLG RMLNGRIDQD
     KMLECLQTLD IDLVLTAHPT EISRRTLIQK YSAVVDCLAT MENPQLTERE KKQNHLRLRQ
     LIAQIWHTNE IRHERPTPVD EARWGLSTIE ASLWQAIPDF LRQLNEQVEE RTGKQLPSDI
     APIRFSSWMG GDRDGNPFVT AKVTQEVLDR NRHTAARLYL KDVVLLVNEL SMEEANEELL
     ALTDNSHEPY RVVLRELRQK LRDTIDYLNA RLEGHSPEVD LDSLIWHEDD LKQPLTLLYR
     SLTESGMSLI ANGLLLDMLR RLACFGIHML RLDIRQDAQR HSDVIAELTR YLGLGDFDHW
     DEHEKQAFLL RELSGKRPLI PHNWEPSAEV AEVISTVRLI ASQSPKALGS YVISMASQPS
     DVLTVLLLLK EAGCQHPMRV VPLFETLEDL NNAASCISAL FAIDWYRGYC KGSQEVMIGY
     SDSAKDAGVM AAAWAQYSAQ EKLVKVCNQA DIKLTLFHGR GGTIGRGGGP AHKAILSQPP
     GSVDGRIRVT EQGEMIRFKF GLPKLAVQSL ALYTSAVMEA TLLPPPEPKP EWREAMERLA
     SDSVTAYRAI VREEPDFVAY FRAATPEVEL GKLPLGSRPA KRRVDGGIES LRAIPWIFAW
     SQNRLMLPAW LGAGEALQQA ADRGELTLLR EMEQQWPFFE TRISMLEMVY AKAEPNLAKY
     YETCLVPQEL HHLGEALRSR MATGIKVVLE LTQSDALMSH TPWNRESVEL RNPYIDPLNF
     LQAELLARTR KEQAGSSNVE LALMLTIAGV AAGMRNTG
//