ID   B7K0F0_RIPO1            Unreviewed;      1024 AA.
AC   B7K0F0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-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=PCC8801_3469 {ECO:0000313|EMBL:ACK67434.1};
OS   Rippkaea orientalis (strain PCC 8801 / RF-1) (Cyanothece sp. (strain PCC
OS   8801)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Rippkaea; Rippkaea orientalis.
OX   NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK67434.1, ECO:0000313|Proteomes:UP000008204};
RN   [1] {ECO:0000313|Proteomes:UP000008204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204};
RX   PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(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;
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; CP001287; ACK67434.1; -; Genomic_DNA.
DR   RefSeq; WP_012596693.1; NC_011726.1.
DR   AlphaFoldDB; B7K0F0; -.
DR   STRING; 41431.PCC8801_3469; -.
DR   KEGG; cyp:PCC8801_3469; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008204; 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:ACK67434.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008204}.
FT   ACT_SITE        194
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        671
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1024 AA;  118369 MW;  48E02B37E1609400 CRC64;
     MSSLLESSSS IVEEINIFST SDLFLRQRLK LVEELWEAVL RAECGQELVD LLKQLRTMCS
     PEGQLTDITQ TPITAVIEQL ELNESIRAAR AFALYFQLIN IVEQHYEQRD QQLTRRANYC
     DIDSKPANNH GESSTNPSIG HHLVERSWMD SENTSEKGGT FHWLFPHLKE LNVPPQQIQR
     LLDQLDIRLV FTAHPTEIVR HTIRRKQRRI VNILRRLDRA EEAFRGMGLS NSWEAQSAIE
     QLTEEIRLWW RTDELHQFKP SVLDEVDYAL HYFDEVLFEV LPQLSQRLQQ SLKSSFPWLR
     PPKNTFCRFG SWVGGDRDGN PFVTPEVTWK TACYQRNMVL KKYLESIRDL TEILSASLHW
     SNVSQDLLDS LERDRVQMPE IYDELAIRYR HEPYRLKLAY IEKRLQNTRD RNNRLANPDQ
     RQQLLYREEE NIYHSGEEFW QELELIKRNL EETGLNCLEL NNLLIQAEMF GFNLTQLDFR
     QDSSRHADAI EEIAEYLNIL PKPYTQLSEA EKTQWLIQEL KTRRPLIPTG MQFKKPENSE
     TVETLQMLRY LQQEFGLEIC QTYIISMTNY VSDVLEVLLL AKEAGLYDPA TSTTTIRIVP
     LFETVDDLKR APEVMEDLFK LPLYRASLAG GYDQLQPSET PSQGAVKSLN LPALQPTNLQ
     EIMVGYSDSN KDSGFLSSNW EIHKAQKALQ NMAQRYGVDL RLFHGRGGSV GRGGGPAYAA
     ILAQPSSTIN GRIKITEQGE VLASKYSLGD LALYNLETVS TAVIQASLLG SGFDDINPWN
     EIMEDLAERA RKAYRGLIYE QPDFLDFFLS VTPIPEISQL QISSRPARRK SGKADLSSLR
     AIPWVFSWTQ SRFLLPAWYG VGTALQSFVD EEPEENLKLL RYFYLKWPFF KMVVSKVEMT
     LSKVDLQIAH HYVRELSKAE DKERFERVFE EISQEYHRTR DVILNITNHQ RLLDSDLSLQ
     RSVQLRNGTI VPLGFLQVAL LKRLRQYSNQ AQSGVIHFRY SKEELLRGAM LTINGIAAGM
     RNTG
//