ID   CAPP_SERP5              Reviewed;         878 AA.
AC   A8GL86;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   10-JUN-2026, entry version 90.
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};
GN   OrderedLocusNames=Spro_4783;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RX   PubMed=19060168; DOI=10.1128/aem.02239-08;
RA   Taghavi S., Garafola C., Monchy S., Newman L., Hoffman A., Weyens N.,
RA   Barac T., Vangronsveld J., van der Lelie D.;
RT   "Genome survey and characterization of endophytic bacteria exhibiting a
RT   beneficial effect on growth and development of poplar trees.";
RL   Appl. Environ. Microbiol. 75:748-757(2009).
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 = phosphoenolpyruvate +
CC         hydrogencarbonate; 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; Evidence={ECO:0000255|HAMAP-
CC         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; CP000826; ABV43876.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8GL86; -.
DR   SMR; A8GL86; -.
DR   STRING; 399741.Spro_4783; -.
DR   PaxDb; 399741-Spro_4783; -.
DR   KEGG; spe:Spro_4783; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   FunFam; 1.20.1440.90:FF:000002; Phosphoenolpyruvate carboxylase; 1.
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   NCBIfam; NF000584; PRK00009.1; 1.
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.
FT   CHAIN           1..878
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000061233"
FT   ACT_SITE        137
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        545
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   878 AA;  98397 MW;  5C09BFB7A807C316 CRC64;
     MNEQYSAMRS NVSMLGKLLG DTIKEALGEH ILDRVETIRK LSKSSRAGNE AHRQELLSTL
     QNLSNDELLP VARAFSQFLN LTNVAEQYHS ISPNGEAASN PEALAQLFTR LKDKKLSTKE
     LQNAVSQLSI ELVLTAHPTE ITRRTLIHKL VEVNTCLSQL DHNDLADYER NKIMRRLRQL
     VAQSWHTDEI RKHRPSPIDE AKWGFAVVEN SLWEGVPAFL REFNEQLENS IDYSLPAEAV
     PVRFTSWMGG DRDGNPNVTA EITRHVLLLS RWKACDLFTR DIQVLVSELS MTECTPELRA
     RAGGDEVQEP YREIMKQLRS QLMSSQAYLE GRLKGERVLK PHDLLVNNEQ LWEPLFACYQ
     SLQACGMSII ANGQLLDTLR RVRCFGVPLV RIDVRQESTR HTEAIAELTR YLGLGDYESW
     SEADKQAFLI RELNSKRPLV PLKWEPSADT QEVLETCRVI AEAPQGSIAA YVISMARTPS
     DVLAVHLLLK EAGCPFALPV APLFETLDDL NNADDVMTQL LNIDWYRGFI QGKQMVMIGY
     SDSAKDAGVM AASWAQYRAQ DALIKTCEKA GVALTLFHGR GGSIGRGGAP AHAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPEVTISSL ALYTGAILEA NLLPPPEPKK EWRALMDDLS
     DTSCKMYRGY VRENPEFVPY FRAATPELEL GKLPLGSRPA KRKPNGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAGLQEA VKAGKQDQLE AMCRDWPFFS TRIAMLEMVF AKADLWLAEY
     YDQRLVDKSL WPLGQQLRDQ LASDIKVVLT IANDAHLMED LPWIAESIAL RNVYTDPLNV
     LQAELLHRSR QQEQPDARVE QALMVTIAGV AAGMRNTG
//