ID   CAPP_GLOVI              Reviewed;         939 AA.
AC   Q7NNJ7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000255|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000255|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000255|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000255|HAMAP-Rule:MF_00595}; OrderedLocusNames=gll0414;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00595};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00595}.
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DR   EMBL; BA000045; BAC88355.1; -; Genomic_DNA.
DR   RefSeq; NP_923360.1; NC_005125.1.
DR   RefSeq; WP_011140417.1; NC_005125.1.
DR   AlphaFoldDB; Q7NNJ7; -.
DR   SMR; Q7NNJ7; -.
DR   STRING; 251221.gene:10757886; -.
DR   EnsemblBacteria; BAC88355; BAC88355; BAC88355.
DR   KEGG; gvi:gll0414; -.
DR   PATRIC; fig|251221.4.peg.421; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   InParanoid; Q7NNJ7; -.
DR   OrthoDB; 9768133at2; -.
DR   PhylomeDB; Q7NNJ7; -.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
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; Lyase; Magnesium; Reference proteome.
FT   CHAIN           1..939
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166596"
FT   ACT_SITE        151
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   939 AA;  107819 MW;  F4D8A53A44903423 CRC64;
     MNWDTPIDLA AAGSPSALSH QSLRDNIELV EQLLRQVAAQ EGGGDLVELL DRLWASHQDR
     TGEGLALIRE LSLEKSVLAI RAFSIYFQLI NIVEQHHERK RLRLQASFSA DTAQPGSFCW
     LFDEMKSLGV STPEIERVLQ QLDVRLVFTA HPTEIVRRTI RTKHRRIVHL LDDLDNALSE
     WQQQQVHTTM LEEIRIWWRT DELHQVRPTV LDEVAHTVHY FEEVLFEAMP RVRSELVRCL
     DMFHPSLTRS LGTFCRFGSW VGSDRDGNPS VNALVTWKTA CHQRSRVLAK YIKSVERLRD
     LLSLAEGNPP QDLLLALEQD QRDLGEVYER YSVVYLQEPY RLKLSYILER LEHTRERNAW
     LEVHGPQRLS QPDEPGWLHY YRHAHELLAE LHLLRQCLRT TGIGCRPLET LIDQVEVFGF
     HLAGLDVRQD STRHEDTLTE VSAKLRLTAT PYAELDEQAR LEWLVRELQT LRPLIPAELP
     FSARTEETIQ TFRMIRRLQK EFGSEICHTY IISMSKQASD LLEVLLLAEE AGLFDPATGT
     GTLMVVPLFE TVEDLRNAPH VLEQLFSLPL YRCYLTCHQN LQEVMLGYSD SNKDSGFLSS
     SWEIFLAQQH IQQVARRHGV QLRIFHGRGG TVGRGGGPSY QAILAQPDGT VSGRIKITEQ
     GEVLASKYSL FELAAFNIET VTAAVIQASV LPTSPPGSRN WELRLQELSD VARRTYRQLV
     YEQEGFIDFF CHVTPIDEIS QLQISSRPSR REGRRDLASL RAIPWVFSWT QSRFLLQAWY
     GLGTALDGFI RCNRERNLAE LRSMYRQWPF FRTLISKVEM TLAKVDLQVA ANYVQELLPK
     EHEHTGECIF ALIAAELERT RECVLAITEH RQLLEDNPPL QRSIALRNAT IAPLGYLQAT
     LLKYLRYENR QPRSYSRNEL LRGALLTING IAAGMRNTG
//