ID   CAPP_ALISL              Reviewed;         876 AA.
AC   B6EMN4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=VSAL_I2754;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
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; FM178379; CAQ80438.1; -; Genomic_DNA.
DR   RefSeq; WP_012551194.1; NC_011312.1.
DR   AlphaFoldDB; B6EMN4; -.
DR   SMR; B6EMN4; -.
DR   STRING; 316275.VSAL_I2754; -.
DR   PRIDE; B6EMN4; -.
DR   EnsemblBacteria; CAQ80438; CAQ80438; VSAL_I2754.
DR   KEGG; vsa:VSAL_I2754; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; 398146at2; -.
DR   Proteomes; UP000001730; Chromosome 1.
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.
FT   CHAIN           1..876
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000129824"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        543
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   876 AA;  99129 MW;  D556F91F1E5A96E9 CRC64;
     MNEKYAALKS NVSMLGHLLG NTIRDAHGEE LLAKVETIRK LSKTARAGSD NDRNALIEEI
     KSLPNDQLTP VARAFSQFLN LTNMAEQYHT ISRHCEEHVC EPDAISSLFS KLSQNNISKL
     DTVQAVRELN IELVLTAHPT EIARRTMINK LVKINECLSK LELSDISFSE REKTERRLEQ
     LIAQAWHSDV IRQERPTPLD EAKWGFAVVE NSLWQGIPDF LREFDQRLEN HLGEGLPIDA
     RPVHMSSWMG GDRDGNPFVT HTITREVMLL SRWKAADLYL KDVNELISEL SMVKCTDEVR
     KLAGDQHEPY RAILKQLRTL LNDTLENLDA QMKGELTNNK PILRNAEQLW LPLHACYQSL
     HACGMGIIAE GSLLDTLRRV KAFGAHLVRL DIRQESTRHS NVLSELTRYL GIGDYDQWSE
     QDKISFLVNE LSSKRPLLPR DWTPTAEVQE VIDTCKIVAE QSKEALGSYV ISMARTASDV
     LAVHLLLQEA GCPFRMDVCP LFETLDDLNR SKEVMEQLFS IDWYRGFIQN HQMVMIGYSD
     SAKDAGVMSA GWAQYSAMEA LVDVCEKESI ELTLFHGRGG TIGRGGAPAH AALLSQPPKS
     LKGGLRVTEQ GEMIRFKLGL PEVAVNSFNL YASAILEANL LPPPEPKQEW RDLMEVLSEV
     SCEAYRNIVR GEKDFVPYFR AATPELELGK LPLGSRPAKR NPNGGVESLR AIPWIFSWSQ
     NRLVLPAWLG AGEAIQYSID KGHQELLEEM CREWPFFSTR LGMLEMVYTK CNPQMSEYYD
     QRLTDKSLWP LGVRLRNQLQ ADIKAVLNVE NSDHLMESDP WGSESIRLRN IYVDPLNMLQ
     AELLYRTRQQ EETSPELEEA LMVTIAGIAA GMRNTG