ID   D0KZG1_HALNC            Unreviewed;       938 AA.
AC   D0KZG1;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
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=Hneap_0998 {ECO:0000313|EMBL:ACX95834.1};
OS   Halothiobacillus neapolitanus (strain ATCC 23641 / c2) (Thiobacillus
OS   neapolitanus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Halothiobacillaceae; Halothiobacillus.
OX   NCBI_TaxID=555778 {ECO:0000313|EMBL:ACX95834.1, ECO:0000313|Proteomes:UP000009102};
RN   [1] {ECO:0000313|EMBL:ACX95834.1, ECO:0000313|Proteomes:UP000009102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23641 / c2 {ECO:0000313|Proteomes:UP000009102};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Davenport K., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Kerfeld C., Cannon G., Heinhort S.;
RT   "Complete sequence of Halothiobacillus neapolitanus c2.";
RL   Submitted (OCT-2009) 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; Evidence={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; CP001801; ACX95834.1; -; Genomic_DNA.
DR   RefSeq; WP_012823870.1; NC_013422.1.
DR   AlphaFoldDB; D0KZG1; -.
DR   STRING; 555778.Hneap_0998; -.
DR   KEGG; hna:Hneap_0998; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000009102; 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; 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.
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:ACX95834.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009102}.
FT   ACT_SITE        147
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        595
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   938 AA;  106985 MW;  7103A2F2471FFF93 CRC64;
     MKKNSKDNDK ALRARVRLFG NLLGEVLKEQ TGDHVFDTVE TLRRGFIKLR LKHNPKLHAK
     LMVLLRTLDP DTLNFVVRAY NLYFSLVNIA EEDFMHQHRR KQVRLGLRLW RGSFYDTMRE
     FSKQGMSPDD LQTLLNRLIY MPVFTAHPTE AKRRTVMDLQ RKIFLLCAEL DHPEAKGIER
     DRLHQQVKSV ILSLLKTNEV RTTRPEVHDE IRLGLYYFST SIFDAVPLAY RYLERAVDVN
     FNEKFPDAPV TVPSLFRFGS WIGGDRDGNP YVTHEVTTFA VCSATQTILQ EYLDRLAGMD
     RVLTHSCRLC PEIDLEGLGL HQDAVELGLA SPENSGDSFF TEEPYRLKLR IIGQRLKHNL
     DYVTALLDKK PINLSAHAYA HKDQFLSDLY RIRDTLISTG DQLLADGEIK DLIRLAETFG
     WHLFKLDIRQ ESTRHTQTVA DILKQLQPKT DYMALDEAGR MTLLTQLINK SRHKAIDMAA
     LSAESAETLE VFKVKRELID TISRECFGTY VISMTHAASH VMEVMFLAVL AGLAGKRKSQ
     WFCDIQISPL FETIEDLHQI ENVLSVLFEN PVYRELIRVS GDLQEAMLGY SDSCKDGGSL
     ASVWSLYNAQ KRVLSITQKN GIECRLFHGR GGTVARGGGP THESILSLPA GTVEGQIKFT
     EQGEVLSSKY SNTETAIYEI TMGATGLMKA SAHLVMENNP APAEHEQVVA ELATYGEKAY
     RELTDETPFF FNYFFEATPV RELGLLNIGS RPASRKVGDL SKASVRAIPW VFGWSQSRHT
     LPAWYGIGSA LRAWRQSHKD QPELLHTLFN EWPFFHSMLR NTQLSLTKGE MTIAREYASL
     VADQAQALPV YDKISTEYYR TLDELLRVAR VDSLVEIDEY IGTSMMRRNP YLDVLNHIQI
     VLLRRYRDDS EPEAERQKWL LPLLRSINAI ASGMRNTG
//