ID   Q3JD13_NITOC            Unreviewed;       957 AA.
AC   Q3JD13;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=Noc_0770 {ECO:0000313|EMBL:ABA57283.1};
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261 {ECO:0000313|EMBL:ABA57283.1, ECO:0000313|Proteomes:UP000006838};
RN   [1] {ECO:0000313|Proteomes:UP000006838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107
RC   {ECO:0000313|Proteomes:UP000006838};
RX   PubMed=16957257; DOI=10.1128/AEM.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA57283.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3JD13; -.
DR   STRING; 323261.Noc_0770; -.
DR   KEGG; noc:Noc_0770; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   InParanoid; Q3JD13; -.
DR   Proteomes; UP000006838; 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:UP000006838}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        614
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   957 AA;  109006 MW;  F664130E0D8F8A45 CRC64;
     MTSMKPQTPE TNPALQDQTG NTTPWRDKEL RARVKLFGNL LGQVIQNQSG EKVFAAVEAL
     RKGYINLRKK ENSDKRIQLL RLIDTLNVEK ITQVVRAFSI YFSLANIAEE AYQHRQRQRR
     IDAGGPLWRG SFEETLRELR KSGISPEQLQ IMLDNLAYIP VITAHPTEAK RRTVMEHLRK
     IFLASKLLDE TRLSQREEET LHRQLERQIQ VLWKTDEVRA HRPQVQDEII NGLFYFKVSL
     FQAVPETYRQ LEEAINKVYG DMLPESTTLR VPSFLHFGSW IGGDRDGNPN VTPEVTAMAV
     RLQMRMALQH YIACITKLTR ILTHSIPLIR PSTALTESIN QDLSDCPETF RGDPDRFSRE
     PYRRKLYLMR YRLMDNLRAV ERYLLPEIQP TPPQGVGYPS EEKFLEDLCL LRDSLSSHGD
     GNIAAGELQD LIRLVESFGF YLLKLDVRQE SGRHTEAVAE LVKHLDLHPS YLDLSETERL
     GLLSEQLARE EETTIQRERL TPATRETLDL FHVMAQMRQE VSPRVFGHYV ISMTHAASHV
     MEVMYLGYLA GLAGRRRGQW HCGLQISPLF ETIEDLEHIE PVMTALLDDP SYRALLQAAG
     NQQEVMIGYS DSCKDGGILA SSWKLYDAQK KVTGLTDSRG VDCRIFHGRG GTIGRGGGPT
     FDAILSQPQG TVHGQIKFTE QGEVLSSRYS NPETAIYELN MGISGLIKAS TCLVQPPQEE
     KRDYLGIIDS LVETGEQTYR EFTEQTSGFQ DYFYEATPVN EIGLLNIGSR PPHRKKGDRS
     KNSVRAIPWV FGWAQARHTF PAWYGIGSAL EKWRAGAPDR LAKLQTMYEE WPYFRALLSN
     TQMSLAKAEL HIAQQYAGLC LDPETGQKIF ALLSAEYQRT VTQVLHIVGA HTLLEENPPL
     ALSLQRRDPY LDPLNHIQLT LLKRTRDPRI TPEEREAWLD PLLRSINAIA AGMRNTG
//