ID   D5C581_NITHN            Unreviewed;       962 AA.
AC   D5C581;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
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   OrderedLocusNames=Nhal_2213 {ECO:0000313|EMBL:ADE15304.1};
OS   Nitrosococcus halophilus (strain Nc4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE15304.1, ECO:0000313|Proteomes:UP000001844};
RN   [1] {ECO:0000313|Proteomes:UP000001844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nc4 {ECO:0000313|Proteomes:UP000001844};
RG   US DOE Joint Genome Institute;
RA   Campbell M.A., Malfatti S.A., Chain P.S.G., Heidelberg J.F., Ward B.B.,
RA   Klotz M.G.;
RT   "Complete genome sequence of Nitrosococcus halophilus Nc4, a salt-adapted,
RT   aerobic obligate ammonia-oxidizing sulfur purple bacterium.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; CP001798; ADE15304.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5C581; -.
DR   STRING; 472759.Nhal_2213; -.
DR   KEGG; nhl:Nhal_2213; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001844; 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:SF46; 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   Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        619
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   962 AA;  109063 MW;  D2E4C47AA3F2DC3C CRC64;
     MTPMMKQIPE AKPAPIASVS PDQTKNATPW RDKELRARVK LFGNLLGQVI QAQSREKVFA
     AVEALRKGYI NLRKKENPDK RIQLLRLISK LDVETLTQVV RAFSIYFSLA NIAEEAYQHR
     QRQRRIDAGG PLWRGSFEET LQEVRNGGVG PGQLQILLDS LAYIPVITAH PTEAKRRTVM
     EHLRKIFLTS KLLDEARLSQ REEEALHRQL ERQIQVLWKT DEVRAHRPQV RDEIINGLFY
     FKVSLFQAVP ETYRQLEEAI HKVYGDDLPE NTTIRVPSFL HFGSWIGGDR DGNPNVKPEI
     TAMAVRLQMR MALRHYLERI GELMRILTHS IPLIQPSTAL MDSINQDLND CPEALLGNPT
     RFSHEPYRRK LYLMRYRLLD NLRAVELHLK PESGLSPPSG VGYPSEDEFL QDLYLIRDSL
     INHGDGNIAA GELQDLIRLV ESFGFYLLKL DIRQESSCHT EAVAELVKQA GLHPAYLDLS
     ETERQQLLSE QLAREEGVPI DREQLTPPTR ETLEIFDVMA QMRREVSPRV FGTYVISMTH
     AASHVLEVMF LGHLAGLAKH QQGQWHCDLQ ISPLFETIED LEHIEPVMTA LLDDPSYQAL
     LQASGNQQEV MIGYSDSCKD GGILASSWKL YEAQKKVTAL TGDRGVDCRI FHGRGGTIGR
     GGGPTFDAIL SQPRGTVHGQ IKFTEQGEVL SSRYSNTETA IYELDMGISG LIKASACLVQ
     PPQEEKRDYL GVMDFLAEAG ERAYRELTEE TPGFQDYFYE ATPVNEIGLL NIGSRPSHRK
     KGDRSKASVR AIAWVFGWAQ ARHTFPAWYG IGSALEQWRA GAPDRLAKLQ AMYQEWPYFR
     AMLSNIQMSL AKAELRIAQQ YAELCLDPET GERIFAMLSA EYQRTVTQVL HIVGAHTLLE
     ENPSLALSLR RRDPYLDPLN HIQLTLIQRT RDPLLTPVER QAWIDPLLRS INAIAAGMRN
     TG
//