ID   D5BVY9_NITHN            Unreviewed;       932 AA.
AC   D5BVY9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   24-JAN-2024, entry version 67.
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_2483 {ECO:0000313|EMBL:ADE15568.1};
OS   Nitrosococcus halophilus (strain Nc4).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=472759 {ECO:0000313|EMBL:ADE15568.1, 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; ADE15568.1; -; Genomic_DNA.
DR   RefSeq; WP_013033428.1; NC_013960.1.
DR   AlphaFoldDB; D5BVY9; -.
DR   STRING; 472759.Nhal_2483; -.
DR   KEGG; nhl:Nhal_2483; -.
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: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   Reference proteome {ECO:0000313|Proteomes:UP000001844}.
FT   ACT_SITE        157
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        591
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   932 AA;  106722 MW;  D3175662C7E2BFD4 CRC64;
     MKHEYKLDIK AEESGLSEPL AKQLTLLGTL LEQAIRDQAG PKMLNLMGKL HQLCGQVDTQ
     DNATLCEGAD TQIQKLSRDQ IVWLLHAYTS FFHLANQAEQ QEIIRINWER VRQSRIDKPR
     PESIDEAIHH LQKQGYAREQ VLQLLGQLDI QPTLTAHPTE ARRRSILFKQ QRISGLLAGL
     NQYSSTTPPE TERILDDLYN QIALLLATDE VRAERPTVKQ EIHQGLYFMR IAIWEVAVQI
     YRDTQRALQQ YYGEAPDFPP FLHYRSWIGG DRDGNPHVTP EITRWTIITH RETALRRYCT
     ELQELYHELS LSERQVGIPP ALYRSLEQDA RETTLGHKFS EQLQREPYRL KISYMMARLG
     KLLKPPNQTE TGENTYNSKR FIEDLQLLKR CLEESGFGKI SRHGRLGRLL ILTQTFGFHL
     AALDVRQHSH IHEKAVAALL QIAGITRDYL ALSEKERLAV LSAQLQKPHP LRVPNSVLPE
     STQQVLETFA VIRDAIAQEP EAIGSYVISM THTISDLLEV MLLAKEAQLW QLQDGKVICP
     LDFVPLFETI EALEAADKRM LALIKHPIYR QQIAARGHFQ EIMLGYSDSS KDGGYWMANW
     ALHKAQKRLG KLCHQQKIDF RLFHGRGGTV GRGGGRTSQT AILAMPPAVH NGRIRFTEQG
     EVISFRYALP AMARRHTEQI VNAMIQATAV AAQSGDKPSD DSYHEDLMER IAQQAMGAYR
     TLIEQDGFWS WYTQVTPIEH ISHLPIASRP ISRTSATEVD FKNLRAIPWV FAWTQTRYLV
     PGWFGLGQAL QKIMGDETLQ ETLQKMYQQW PFFNTVIDDA QREMARARLK TASHYARLAN
     QNETRFHDII VADFEKARKI ILEMSGQQEL LDNTPTIQKT IIFRNPYTDV LNLLQIELMK
     RYRQAPENEK GLLRQALFLS LNGIAAAMQS TG
//