ID   B8HVC9_CYAP4            Unreviewed;      1018 AA.
AC   B8HVC9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 85.
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=Cyan7425_2220 {ECO:0000313|EMBL:ACL44581.1};
OS   Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC   Cyanothece.
OX   NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL44581.1};
RN   [1] {ECO:0000313|EMBL:ACL44581.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL44581.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA   Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT   "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL   Submitted (JAN-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;
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; CP001344; ACL44581.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8HVC9; -.
DR   SMR; B8HVC9; -.
DR   STRING; 395961.Cyan7425_2220; -.
DR   KEGG; cyn:Cyan7425_2220; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
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:ACL44581.1}.
FT   ACT_SITE        209
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        665
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1018 AA;  117957 MW;  D6FEDEE29B0DB992 CRC64;
     MTSTVPLSEQ DQILSNRREQ ALRNRMQVIE DLLEAVLQTE CGQTLVDLLR QLRALCSPEG
     QVRRALDEEV LRLIEKLDFN EAIRAARSFA LYFQLINIVE QHYEQQESLY RTHPESGHPL
     PDLISHISGE SFPDKSFSGQ NFSAHNNTVD VRGGLTERVE HSLYEATSLE RHQGTFAWLF
     PHLWQQNVPP RYLQNLIDQL DIKLVFTAHP TEIVRQTIRD KQRRIARILE QLDRVEATLG
     SRSGVEMQNL HEQLIEEIRL WWRTDELHQF KPQVLDEVEY SLHYFKEVVF EIIPQLYRRI
     TQSLQQSFPN LRPPRHNFCK FGSWVGADRD GNPSVTPEVT WETACYQRDL VLEKYTKSVE
     KLINVLSLSL HWCDVLPDLL DSLEQDQQQF PELYEQLSAR FRHEPYRFKL SYVLRRLENT
     RDRNRQLQNG YYPFSTDSSG YGDLQIYRKG EEFLAELLLI QRNLQATNLS CRQLEDLICQ
     VEIFGFNLAQ LDIRQESSCH SEALNEIITY LQILPRPYNE LSEGERTEWL VKELQTRRPL
     IPAELPFSER TREIIETLRM VRRLQQEFGP DICKTYVISM SHEASDLLEV LLLAKEAGLY
     DPVTGTGNLQ VVPLFETVED LKKAPTVLTQ LLELPFYRAY LDSDCPSADV PPLQEVMLGY
     SDSNKDSGFL SSNWEIYKAQ QSLQHTAERY GVALRIFHGR GGSVGRGGGP AYAAILAQPG
     RTIDGRIKIT EQGEVLASKY SLPELALYNL ETITTAVIQA SLLRTSIDEI QPWHEIMEEL
     ALRSRQHYRQ LIYEQPDFVD FFHQVTPIEE ISQLEISSRP SRRGGKRTLT SLRAIPWVFS
     WTQSRFLLPA WYGVGTAIQD FLAEKPVEHL SLLQYFYFKW PFFRMVISKA EMTLAKVDLQ
     IAQHYVRELT HPEDRERFAP LYDQIAQEYY RTCELILTIT GHKRLLDGDP DLQRSVQLRN
     GNIVPLGFLQ VLLLKRLRQH QSQTSSGALL RSRYSKGELR RGALLTINGI AAGMRNTG
//