ID   E4NG02_KITSK            Unreviewed;       931 AA.
AC   E4NG02;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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:BAJ30432.1};
GN   OrderedLocusNames=KSE_46510 {ECO:0000313|EMBL:BAJ30432.1};
OS   Kitasatospora setae (strain ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304
OS   / NBRC 14216 / KM-6054) (Streptomyces setae).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=452652 {ECO:0000313|EMBL:BAJ30432.1, ECO:0000313|Proteomes:UP000007076};
RN   [1] {ECO:0000313|EMBL:BAJ30432.1, ECO:0000313|Proteomes:UP000007076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33774 / DSM 43861 / JCM 3304 / KCC A-0304 / NBRC 14216 /
RC   KM-6054 {ECO:0000313|Proteomes:UP000007076};
RX   PubMed=21059706; DOI=10.1093/dnares/dsq026;
RA   Ichikawa N., Oguchi A., Ikeda H., Ishikawa J., Kitani S., Watanabe Y.,
RA   Nakamura S., Katano Y., Kishi E., Sasagawa M., Ankai A., Fukui S.,
RA   Hashimoto Y., Kamata S., Otoguro M., Tanikawa S., Nihira T., Horinouchi S.,
RA   Ohnishi Y., Hayakawa M., Kuzuyama T., Arisawa A., Nomoto F., Miura H.,
RA   Takahashi Y., Fujita N.;
RT   "Genome sequence of Kitasatospora setae NBRC 14216T: an evolutionary
RT   snapshot of the family Streptomycetaceae.";
RL   DNA Res. 17:393-406(2010).
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; AP010968; BAJ30432.1; -; Genomic_DNA.
DR   RefSeq; WP_014137731.1; NC_016109.1.
DR   AlphaFoldDB; E4NG02; -.
DR   STRING; 452652.KSE_46510; -.
DR   KEGG; ksk:KSE_46510; -.
DR   PATRIC; fig|452652.3.peg.4639; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_11; -.
DR   Proteomes; UP000007076; 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:BAJ30432.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007076}.
FT   ACT_SITE        144
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        589
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   931 AA;  103331 MW;  90BDCB858FE97CA8 CRC64;
     MTAPVPTPAD SPSSIADADN AALRADIRRL GDLLGETLVR QEGPELLGLV EQVRLLSRTD
     GEATAQLLAE IDLDTAAKLV RAFSTYFHLA NVTEQVHRGR EFAARRALEG SVLSQTVDQL
     KEADPKHLAD TLANLSVRPV FTAHPTEAAR RSVLNKLRRV GELLERIHRE QAATGRVDSA
     RQTSARRQAD RRLAEVIDLL WQTDELRIAR PEPTDEARNA VYYLDELYRE AVPEVLEELH
     EELARVGLTL PEGVRPLTFG TWIGGDRDGN PNVTPRVTWD VLNLQHEYGI KDALEAVDDL
     RASLSTSVRL AGASEELLAS LDADLAHLPE LSPRYKRMNA EEPYRLKATC IRIKLENTRD
     RLAAGTAPTP GRDYVGTRDL IADLRLVQDS LRAHRGGLIA DGRLARTIRT IEAFGLQLAT
     MDVREHAEAH HHALGQLFDR LGEEAWRYTD MPREYRQRLL SKEMRSRRPL APTPAPLDAA
     GAKTLGVFTT IREGFERFGD EIVESYIISM CQGADDVFAA AVLAREAGLI DLHAGIAKIG
     IVPLLETTDE LQEADRILDE MLSDPSYRLL VSLRGDVQEV MLGYSDSSKF GGITTSQWEI
     HRAQRRLRDV AHRYGIRLRL FHGRGGTVGR GGGPSHEAIL AQPWGTLEGE IKVTEQGEVI
     SDKYLLPSLA RENLELTLSA TLAASALHTA PRQAPEELAR WDAAMDRVSE AAHTAYRALV
     EQEDLPKYFF AATPVDQLAS LHLGSRPSRR PDSGAGLDGL RAIPWVFGWT QSRQIVPGWY
     GVGSGLAAAR EAGLGDVLDE MHGNWHFFRN FLSNVAMTLA KTDLRIARHY VEQLVPAELH
     HVFEQIVAEH DLTLREVLRL TGESELLEHN DVLKQTFTVR DAYLDPISYL QVALLRRQRE
     EVAAGRPEDP LRARALLLTV NGIAAGLRNT G
//