ID   CAPP_PHOLL              Reviewed;         878 AA.
AC   Q7MAX5;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=plu4746;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01) (Photorhabdus luminescens subsp. laumondii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
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; 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; BX571874; CAE17118.1; -; Genomic_DNA.
DR   RefSeq; WP_011148814.1; NC_005126.1.
DR   AlphaFoldDB; Q7MAX5; -.
DR   SMR; Q7MAX5; -.
DR   STRING; 243265.plu4746; -.
DR   GeneID; 24168737; -.
DR   KEGG; plu:plu4746; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002514; 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_0000166608"
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;  98823 MW;  A943F294497764EE CRC64;
     MNQQYSAMRS NVSMLGKLLG DTIKEALGED ILDKVETIRK LSKSSRAGNE AHRQQLLSTL
     QNLSNNELLP VARAFNQFLN LTNVAEQYHS ISPHGEAASN PVALAKLFTR LKEKNFNNGD
     LKKAVNELSI ELVLTAHPTE IARRTLIHKL VAVNTCLSQL DHDDLADYER NNIMRRLRQL
     VAQSWHTDEI RKIRPTPIDE AKWGFAMVEN SLWEGVPAFL REFNEQLEES IDYSLPVEAV
     PVRFTSWMGG DRDGNPNVTA EVTRHVLLLS RWKAADLFLK DIQVLVSELS MSECTPEVRK
     LAGGDEILEP YREIAKKLRT QLSNTLTYLE KQLKGEQVLP PTDLLVDNEQ LWQPLYACYQ
     SLKTCGMEII ANGQLLDILR RIRCFGLSLV RIDVRQESTR HTTAISELTQ YLELGDYASW
     SEEEKQAFLL YELHSKRPLI PHNWQPSAET QEVFATCKVI AESPQDAIAA YVISMAKAPS
     DVLAVHLLLK EAGCPFTLPV APLFETLDDL NNAENIIQQL MNIQWYRELI HDKQMVMIGY
     SDSAKDAGVM AAAWAQYRAQ DALINVCEKE GITLTLFHGR GGTIGRGGAP AHAALLSQPP
     GSLKGGLRVT EQGEMIRFKF GLPQVTISSL ALYASAILEA NLLPPPEPKP EWHQVMDTLS
     DVSCKMYRDY VREQPDFVPY FRAATPEQEL AKLPLGSRPA KRHPAGGVES LRAIPWIFAW
     TQNRLMLPAW LGAGAALQQV VNDGKQDVLA EMCRDWPFFT TRIGMLEMVF AKADLWLAEY
     YDHRLVDKNL WPLGQKLRKQ LSADIKTVLA ISKDEHLMAD LPWIAESIAL RNVYTDPLNV
     LQVELLLRSR QQQYSDPQVE QALMVTIAGI AAGMRNTG
//