ID   B8GNA5_THISH            Unreviewed;       947 AA.
AC   B8GNA5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=Tgr7_0875 {ECO:0000313|EMBL:ACL71966.1};
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL71966.1, ECO:0000313|Proteomes:UP000002383};
RN   [1] {ECO:0000313|EMBL:ACL71966.1, ECO:0000313|Proteomes:UP000002383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL71966.1,
RC   ECO:0000313|Proteomes:UP000002383};
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71966.1; -; Genomic_DNA.
DR   RefSeq; WP_012637454.1; NC_011901.1.
DR   AlphaFoldDB; B8GNA5; -.
DR   STRING; 396588.Tgr7_0875; -.
DR   KEGG; tgr:Tgr7_0875; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_6; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000002383; 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   Pyruvate {ECO:0000313|EMBL:ACL71966.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002383}.
FT   ACT_SITE        153
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        602
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   947 AA;  107865 MW;  CF7072E6F1B7A428 CRC64;
     MKEDQLMPVN LPPRDKELRA RVKLFGNLLG KVLKRLEGRR ALAAVETLRK GFIALRKQDD
     PAKRAKLMAF IDKLDADSLE LIIRAFSTYF SLANIAEEDF LYRERRRQVS EGGPLWVGSF
     DHTLRELHEQ GIPADSLQRL LDQLAYVPVF TAHPTEARRR TVMEAQRRIF LAADRLNDRR
     LGREEREELT QELETRIQVL WRTNEVRVKK PQVQDEIKYG LFYFEESLFN AVPITYRFLE
     KAIRRTYGND EAGNPRVRVP SFLRFGSWIG GDRDGNPNVT PAVTELACRL AMEQVLSEYL
     RRVSALRHEL THSLYMCQPS EAFLESLERD SNIATAVFRG SADRFETEPY RRKLYIMRYR
     LTETLNTVRR RLNGENAVLP ANSAYASAAE MLNDLRLMHD SLVSHGDANV AAGKLTDLIR
     LAETFGFHLF HLDIRQESTV HGQTVAEILK ATGLNEDYDA LSEPERLALL ARLAEAEELP
     RLDGEALSET ARETLEVFHV IGRMRAEVGP EGIGTYVISM THAASHVMEV MFLARLAGLA
     GRNEAGECFC QIRVSPLFET IEDLRHIEEV LEDLLTQPVY ARMLKASGNL QEVMLGYSDS
     CKDGGILASS WNLYEAQQKI LRITGAHHVA CRLFHGRGGT IGRGGGPTHE SILAQPPGTV
     HGQIKFTEQG EVLSYKYSNV ETAVYELSMG ATGLIKASRC LIDNPPMDRR DYLGIMDELA
     ALGEEAYRDL TDRTEGVLDY FYEITPVQEI GQLNIGSRPS HRRKADRSKS SIRAIPWVFG
     WAQSRHTLPA WYGIGTALER WRQNDPSRLA KLQTMYNEWP FFRSLLSNCQ MALTKADMRT
     AEEYARLCHD PELAKRVFGR IHEEFERTVT QVLNVADTQT LLDENPTLAL SLMRRNPYMD
     PLNHIQITLL RRHRELHERQ PEAEQDPWIS PLLRSINAIA AGMRNTG
//