ID   B1VUI2_STRGG            Unreviewed;       909 AA.
AC   B1VUI2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
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=SGR_4379 {ECO:0000313|EMBL:BAG21208.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG21208.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG21208.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
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; AP009493; BAG21208.1; -; Genomic_DNA.
DR   RefSeq; WP_012380562.1; NC_010572.1.
DR   AlphaFoldDB; B1VUI2; -.
DR   GeneID; 6215943; -.
DR   KEGG; sgr:SGR_4379; -.
DR   PATRIC; fig|455632.4.peg.4465; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000001685; 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:BAG21208.1}.
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        567
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   909 AA;  100668 MW;  ADA946B0ECF079FA CRC64;
     MSSADQTPAA SPALRADIRR LGDLLGETLV RQEGQELLDL VERVRALTRT DGEAAAELLG
     DTDLETAARL VRAFSTYFHL ANVTEQVHRA HEMRDRRAAE GGLLARTADR LKDADPEHLR
     ETVKNLNVRP VFTAHPTEAA RRSVLNKLRR IAALLETPAI EADRRRLDLR LAENIDLIWQ
     TDELRVVRPE PADEARNAIY YLDELHTGAV GDVLEDLAAE LERVGVELPA GTRPLTFGTW
     IGGDRDGNPN VTPAVTWDVL ILQHEHGITD ALEMIDHLRG LLSNSIRYAG ATEELLTSLQ
     ADLERLPGIS PRYKRLNAEE PYRLKATCIR QKLVNTRERL AEGTPHRPGC DYLGTAELIA
     DLELIQTSLR AHKGGLFADG RMDRTIRTLG AFGLQLATMD VREHADAHHH ALGQLFDRLG
     EESWRYADMP RDYRQKLLAK ELRSRRPLAP TPAPLDAAGE KTLGVFHTIK QAFERFGPEV
     IESYIISMCQ GADDVFAAAV LAREAGLVDL HAGWAKIGIV PLLETTDELK AADVILDEML
     ADPSYRRLVS LRGDVQEVML GYSDSSKFGG ITTSQWEIHR AQRRLRDVAH RYGVRLRLFH
     GRGGTVGRGG GPSHDAILAQ PWGTLEGEIK VTEQGEVISD KYLIPALARE NLELTVAATL
     QASALHTAPR QSDEALARWD AAMDTVSDAA HSAYRKLVED PDLPAYFLAS TPVDQLADLH
     LGSRPSRRPG SGVSLDGLRA IPWVFGWTQS RQIVPGWYGV GSGLKALREA GLDTVLDEMH
     EHWHFFRNFL SNVEMTLAKT DLRIARHYVD TLVPDELKHV FDAIEAEHAL TVREVLKVTG
     STELLGTSPV LQQTFGIRDA YLDPISYLQV SLLARQRQAA ERGEEPDPLL ARALLLTVNG
     VAAGLRNTG
//