ID   G4QJ22_GLANF            Unreviewed;       869 AA.
AC   G4QJ22;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:AEP28890.1};
GN   OrderedLocusNames=GNIT_0746 {ECO:0000313|EMBL:AEP28890.1};
OS   Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP28890.1, ECO:0000313|Proteomes:UP000009282};
RN   [1] {ECO:0000313|EMBL:AEP28890.1, ECO:0000313|Proteomes:UP000009282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC   {ECO:0000313|Proteomes:UP000009282};
RX   PubMed=22123761; DOI=10.1128/JB.06296-11;
RA   Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT   FR1064T.";
RL   J. Bacteriol. 193:7006-7007(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; CP003060; AEP28890.1; -; Genomic_DNA.
DR   RefSeq; WP_014107765.1; NC_016041.1.
DR   AlphaFoldDB; G4QJ22; -.
DR   STRING; 1085623.GNIT_0746; -.
DR   KEGG; gni:GNIT_0746; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000009282; 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:AEP28890.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009282}.
FT   ACT_SITE        133
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        530
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   869 AA;  97553 MW;  07ACCE68B46571F2 CRC64;
     MNDSLDAQLK DTVRYLGATL GETIEAELGS EWLQKIEQIR QDGRDSYADD TKSTDRLTAL
     FSSLDNQSLL TIGRAFAQFL NLANIAEQEY NSANQRDESL ASSLEKIKTI ATDKEKVIAA
     VKSLNIDLVL TAHPTEVTRR TLIHKHRQLA AQLEAMHAPD LSSKDRGKIK NRIAALISQA
     WHTEEIRSVR PTPVDEARWG FSVIESSLWE AVPEFLRELE EYLKAEFDIT LPLDAKTVQI
     GSWMGGDRDG NPFVTSKVTE EVLMLARRRA AKLFALDMDD LYIELSMNDC NDKLRDMVGD
     AKEPYRAALK AIRNKLEKTR DNLLPLEEWV ANNDELLTPL LACYESLHEC GMAVIAEGVL
     KDTIRRVHCF GVNLLQLDIR QDSDRHADVF SELTRYLGLG DYAQWSEDDK QAFLLRELSS
     KRPLIPRNWQ PSEDVQEVLD TCAVISRHSR ESFGIYIISM AREASDVMAV QLLLKEAGLS
     WPMPVAPLFE TLDDLNNSPK VMRNLLDIDW YRGYIKGRQY VMIGYSDSAK DAGSLAAGWA
     QYESQEALVA LAEEKSVNLT LFHGRGGTIG RGGLPAKAAI HSQPPGSLTG GFRVTEQGET
     IRYKFGMPQL AKRSLSIYAA AVVEAMLCPP PAPKPLWRET ITKMAAQARD NYRGVVREDP
     EFVPYFRVAT PEQELGKLPL GSRPAKRNPQ GGIESLRAIP WIFAWAQTRM VLPSWLGVMK
     AVESVIEDGS EEAVKDMIDN WPFFNSRLSM LDMVFKKAEP HISAAYDARL VPDNLKHFGE
     GLRAELKQSI ASILRILDHT DMMEDDPHGK LSMEIRGGYL EPLHYLQIEL LDRIRKEGSS
     DYNDNDTATL EMAMMVTITG IAIGLRNTG
//