ID   D5CLC0_SIDLE            Unreviewed;       922 AA.
AC   D5CLC0;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
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=Slit_0266 {ECO:0000313|EMBL:ADE10508.1};
OS   Sideroxydans lithotrophicus (strain ES-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Sideroxydans.
OX   NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE10508.1, ECO:0000313|Proteomes:UP000001625};
RN   [1] {ECO:0000313|EMBL:ADE10508.1, ECO:0000313|Proteomes:UP000001625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-1 {ECO:0000313|EMBL:ADE10508.1,
RC   ECO:0000313|Proteomes:UP000001625};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT   "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL   Submitted (MAR-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; CP001965; ADE10508.1; -; Genomic_DNA.
DR   RefSeq; WP_013028407.1; NC_013959.1.
DR   AlphaFoldDB; D5CLC0; -.
DR   STRING; 580332.Slit_0266; -.
DR   KEGG; slt:Slit_0266; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001625; 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   Pyruvate {ECO:0000313|EMBL:ADE10508.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001625}.
FT   ACT_SITE        152
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        583
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   922 AA;  104068 MW;  2545BADBFFF9018B CRC64;
     MNLISAPADI SSKDIPLRDD VRLLGRILGD TLREQEGEET YKLIESVRRA AVRFRKTQDE
     QDGELLEQML DQLSPTETLV VVRAFSYFSQ LTNIAEDLHH NRRHRAHLKA GSPPKDGTLQ
     LALDRLEEKK IDKDTLQSFL NSALVSPVLT AHPTEVQRKS ILDCHLIISS LLANRDRVDM
     TPDDLAENEE ALHRFVLILW QTRMMRTAKL NVRDEIRNGL EYYHYTFLAE IPKLYANLEK
     QLESRFDKDI KVPPLLRVGS WIGGDRDGNP FVTHDVMTDA VREHSILALE YYLNETHLLG
     TRLSLTDRLV EVTPELRKLS DASPDNVFVR LDEPYRRALI LIYSRLTATA KHLGHDTSHL
     RPVDAHAQPY ATAQDFIADL DVMIDSLFKH GAVYLARGRL ANLRRAVEVF GFYLAPLDMR
     QHSAILEQTV SELFSHSSGK ANYSDLDEAG KRSVLLEALQ SGKILLADIK RYSDVPQSEL
     RIMQAAAEIH RRFGHGALPN HIISKTDAVS DMLEVALMLQ QFGLLQDGDT LHVNIIPLFE
     TIEDLRGGAS IMDELFSIPW YRKLLSSRGN TQEVMLGYSD SNKDGGYLTA NWELYKAEVE
     LVKVFAKHGI ELRLFHGRGG TVGRGGGPSY DAILAQPPGS VNGQIRITEQ GEVISSKYSN
     PEIGRRNLET LIAATIEATL LDHPHNADGD PEYMRIMEAL SLDAFAAYRK LVYETPGFTD
     YFFTATPIRE IAELNIGSRP SSRKASDRIE DLRAIPWVFS WGLNRVMLPG WFGFGSAVKQ
     FIQREGDAGL KQLQAMYKNW AFFRGMMSNM DMVLSKSDMG IAWRYAELVQ DIELRDRIFG
     AINNEWEATI EMLFAVTGAT TLLQDNPAFA RSLLTRTPYI DPLNHLQVAL LHRHRAGDND
     EKVKRAIHLT INGIATGLRN SG
//