ID   D9SK99_GALCS            Unreviewed;       922 AA.
AC   D9SK99;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 65.
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=Galf_2512 {ECO:0000313|EMBL:ADL56511.1};
OS   Gallionella capsiferriformans (strain ES-2) (Gallionella ferruginea
OS   capsiferriformans (strain ES-2)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Gallionella.
OX   NCBI_TaxID=395494 {ECO:0000313|EMBL:ADL56511.1, ECO:0000313|Proteomes:UP000001235};
RN   [1] {ECO:0000313|EMBL:ADL56511.1, ECO:0000313|Proteomes:UP000001235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-2 {ECO:0000313|EMBL:ADL56511.1,
RC   ECO:0000313|Proteomes:UP000001235};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Davenport K.W., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Shelobolina E.S., Picardal F., Roden E., Emerson D.,
RA   Woyke T.;
RT   "Complete sequence of Gallionella capsiferriformans ES-2.";
RL   Submitted (AUG-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; CP002159; ADL56511.1; -; Genomic_DNA.
DR   RefSeq; WP_013294431.1; NC_014394.1.
DR   AlphaFoldDB; D9SK99; -.
DR   STRING; 395494.Galf_2512; -.
DR   KEGG; gca:Galf_2512; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_4; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001235; 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:ADL56511.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001235}.
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;  103726 MW;  A8D439C3FBB344B1 CRC64;
     MNLFSAPADI SSKDLPFRED VRLLGRILGD TLREQEGEAT FQLVENVRRS AVRFRKTQDE
     RDGEQLEQML DALSPSETLA VVRAFSYFSQ LTNIAEDLHH NRRHRAHLKA GSSPKNGSLM
     LALDRIEEKQ VSPEAMQAFL DSALISPVLT AHPTEVQRKS ILDCHLIISS LLSNRDRIEM
     TPDELAENEN ALRRFVLILW QTRMLRTAKL TVRDEIRNGL EFYRYTFLTE IPKLYANLEK
     QLEARFDKDI KIPALLKVGS WIGGDRDGNP FVTHDVMQYA VQQHSELAFE HYLNETHILG
     TRLSLTDRLV DVSDELRAMS DASPDNAVSR TDEPYRRALI MIYSRLSATA GKLGHEISHL
     PPVDKAAAPY ATPAQFIADL DVLIESLNRH GAIYLARGRL ANLRRSAEIF GFHLAPLDMR
     QHSAIHEQTV SELLAHSGVM ANYSELDEAA RREILLTTLQ AAKPLMGKID QYSDIAQSEL
     RIMQAAADIH QRFGRAALPN HIISKADAVS DMLELALMLQ QVNLLEGRDA LHINIIPLFE
     TIEDLRSCGP IMDELFAIPY YRQLLACRGN TQEVMLGYSD SNKDGGYITA NWELYKAELE
     LVKVFAKYGV ELRLFHGRGG TVGRGGGPSY EAILAQPPGS VNGQIRITEQ GEVISSKYSN
     PEIGQRNLET LVAATMEATL LHHHGADSAM PEFHRIMEAL SLDAFAAYRK LVYETPGFTE
     YFFTATPIRE IAELNIGSRP SARRASDRIE DLRAIPWVFS WGLNRTLLPG WLGFGSAVKQ
     FIAREGDDGL AQLQTMYREW PFFRGLMSNM DMVLSKTDMG IASRYAALVE DVEMRERIFG
     AIHSEWQDTV ELLFSVTRND ALLQENPSFA RSLLSRTPYI DPLNHLQVAL LEHHRAGNTD
     ELVKRAIHLT INGIATGLRN SG
//