ID   CAPP_NITEC              Reviewed;         933 AA.
AC   Q0AH90;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
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=Neut_1036;
OS   Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101675 / C91 / Nm57;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT   eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(2007).
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; CP000450; ABI59292.1; -; Genomic_DNA.
DR   RefSeq; WP_011634115.1; NC_008344.1.
DR   AlphaFoldDB; Q0AH90; -.
DR   SMR; Q0AH90; -.
DR   STRING; 335283.Neut_1036; -.
DR   KEGG; net:Neut_1036; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001966; 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.
FT   CHAIN           1..933
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025569"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        592
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   933 AA;  106506 MW;  C37860FB1F4D9C87 CRC64;
     MSLNTLANIV PEKDTSLEKD HPLREDIRLL GRMLGDTIRE LEGEPMFDLV ETIRQTAVRF
     RREQDEEAGK ELDTILNHLS HKETTAVVRA FSYFSLLSNI AEDLHHNRRR RAHLRAGSPP
     QDGSVTLALE RVVAKGINTQ QLENFFAEAL ISPVLTAHPT EVQRRSILDY QLKIQRLLKE
     RDRTQLTPNE LRHNEEDLRS AIQTLWQTRV LRSVRLTVQD EIENGLIYYH YTFLKQIPYI
     YAKIEDILER HMDKAAPCIA SFLRIGSWIG GDRDGNPFVT HQIMLHAAER HSALILDYYI
     EEVEKIGQAM SLTERLIKVT SELEGLASTA PGLPASRIDE PYRRVFLGMH TRLIATSRYL
     SPHVGRQYQE NTAEPYADSA EFVHDLDIVI RSLKQHQSNK LAQGAIRDLR RAVDVFGFHL
     ASLDMRQHSK IHEQVVSELY EKNAQDNRNY PDLTRAERAE WLLAELKRSH PLVSSLSDYS
     DITQGELRIL RMAAEIQRRF GHVALPNYII SMATGVIHIL EAALLLKEAG LLQFGEAARS
     TVNIIPLFET IDDLRGCANV MEELFSLPEY RKMLRSRSNL QEVMLGYSDS NKDGGFVTSN
     WEIHKAEIEL TKVFNRHGVR LRLFHGRGGT VGRGGGPSYQ GILAQPPGSV NGQIRLTEQG
     EVIASKYTDP EIGRRNLETL VAATIESTLL DRDAIHCHTP QCYQIMEELS ASAYAAYRDL
     VYKTPNFTQF FQESTPIREI AGLHIGSRPT SRKPSNKIED LRTIPWVFSW SLNRTMIPGW
     YGFGTAVENF VQQAGNTQDV LIQMQKMYRT WPFFQTLLSN MDMVLAKSDL GIASRYAELV
     TDSELRQYVF TAIRTEWELC VKWLFAITGH TELLQDNPTL ARSIRIRTPY IDPMNHLQVE
     LLRRYRSGDD DDAIRRAIHL TINGVATGLR NSG
//