ID   E3FE67_STIAD            Unreviewed;       889 AA.
AC   E3FE67;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, 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   ECO:0000313|EMBL:ADO72670.1};
GN   OrderedLocusNames=STAUR_4892 {ECO:0000313|EMBL:ADO72670.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO72670.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO72670.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72670.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(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; 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; CP002271; ADO72670.1; -; Genomic_DNA.
DR   RefSeq; WP_013376509.1; NC_014623.1.
DR   AlphaFoldDB; E3FE67; -.
DR   STRING; 378806.STAUR_4892; -.
DR   KEGG; sur:STAUR_4892; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_7; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001351; 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:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
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}.
FT   ACT_SITE        150
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        556
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   889 AA;  98975 MW;  64E65CC9CE0F388B CRC64;
     MARIRPVDQP LRRDVRLLGR LLGEVLIEQH GQPLFELEEQ VRHLAIQRRR GPKPGRRAAA
     AELAALLEKL PLDQAELVLR AFSVYFQLAN LAEQHHRIRR TRGHASAAEA TAQRGSLEAA
     FRTLKDAGVS AGKVREALQG MAVTLTLTAH PTQAARRTLL EKLYRIERLM EERDRCQLTP
     QETADNLESV REELTALWQS DELRRMRPTV GDEVKNALWY VEEVLADQLA RLPELFAWAF
     ERAYGEALGH VASPVRVHSW VGGDMDGNPL VTPEVLADTL RAHRARGLRM LLRDVEALGA
     ALSQSDRRAS LPEELRRSLE KDGALLPEVA ERQGPRTAGE PWRRKLRFME ARLLLALQYV
     EGRRGGHTEP MAAQAYRSPS AFLEDLELIE RTLVEVKSSR AGVRQVRRVM ERVRSLGFHL
     AELEFRVPAE DVLSARASLN GGPAPSEGGA RLLAILDRVR EAQSESGEEC CRTFIMSMAS
     TAEDVLAAFE CAKHAGLWDE ARGCATVDIV PLFEQLGALD GGPEVLKTLF AEPAYRRHLD
     ARGVQEVMVG YSDSGKEVGL LAASAALQRA QIALARVAKE AGVPLRLFHG RGESVARGGG
     PAQQAILSLP QGSLAGGYKA TEQGEALDHK YARPELARRS LELVLAGVLL HTMDAQPRPP
     EEDEATFRQV FDALAEKGRR EYRALVWEDP RFVEFFTAAT PVEEISALPI GSRPSKRKAG
     GLESLRAIPW VFAWTQNRAI LPGWYGVGSA LEEYAAKPEG LALLKRMYRE WPFFRTVIDN
     VTMVLAKSDI AIASRYATLA PASTRPLWRL IRAEHARTRR QVKRLTGEER LLDHNPRLQR
     SIALRNPYVD PMSFLQVELL RRKRAGEPDC DRPLLLTLNG IAAGLRNTG
//