ID   CAPP_SYNY3              Reviewed;        1034 AA.
AC   P74299;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=sll0920;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; BA000022; BAA18393.1; -; Genomic_DNA.
DR   PIR; S76134; S76134.
DR   AlphaFoldDB; P74299; -.
DR   SMR; P74299; -.
DR   DIP; DIP-48802N; -.
DR   IntAct; P74299; 5.
DR   STRING; 1148.gene:10499269; -.
DR   PaxDb; 1148-1653480; -.
DR   EnsemblBacteria; BAA18393; BAA18393; BAA18393.
DR   KEGG; syn:sll0920; -.
DR   eggNOG; COG2352; Bacteria.
DR   InParanoid; P74299; -.
DR   PhylomeDB; P74299; -.
DR   BRENDA; 4.1.1.31; 6192.
DR   Proteomes; UP000001425; 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..1034
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166642"
FT   ACT_SITE        203
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        680
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1034 AA;  118940 MW;  76DF6061BAB7235D CRC64;
     MNLAVPAFGL STNWSGNGNG SNSEEESVLY QRLKMVEELW ERVLQSECGQ ELVDLLTELR
     LQGTHEAITS EISEEVIMGI TQRIEHLELN DAIRAARAFA LYFQLINIVE QHYEQNEQQR
     NRWEASQETN FYEQAGNEEE MVPPSRLGAS TEPLPVGIDQ NELQASVGTF HWLMRELKRL
     NVPPQHIQNL LDHLDIRLVI TAHPTEIVRH TIRRKQRRVD RILRKLDQLQ GSVTGRDWLN
     TWDAKTAIAQ LTEEIRFWWR TDELHQFKPT VLDEVDYSLH YFDEVLFDAV PELSKRLGQA
     IKETFPHLRA PRANFCYFGS WVGGDRDGNP SVTPEVTWQT ACYQRGLVLG KYLFSLGELV
     AILSPSLHWC KVSQELLDSL ERDRIQLPEI YEELSLRYRQ EPYRMKLAYV TKRLENTLRR
     NNRLANPEER QTMITMPAEN HYRTGEELLE ELRLIQRNLT ETGLTCLELE NLITQLEVYG
     FNLAQLDFRQ ESSRHAEAIA EIAEYMGVLT TPYEEMAEED KLAWLGVELQ TRRPLIPQEM
     PFSERTRETI ETLRTLRHLQ MEFGVDICQT YIISMTNDAS DVLEVLLLAK EAGLYDPATA
     SNSLRIVPLF ETVEDLKNAP GIMDSLFSLP FYRATLAGSY HSLKELQNQP PDYYQIPTTT
     ALLNPGNLQE IMVGYSDSNK DSGFLSSNWE IHKAQKSLQA VAQSHRVILR LFHGRGGSVG
     RGGGPAYKAI LAQPAGTVDG RIKITEQGEV LASKYSLPEL ALYNLETLTT AVIQASLLKS
     SFDFIEPWNR IMEELACTAR RAYRSLIYEE PDFLDFFLTV TPIPEISELQ ISSRPARRKG
     GKADLSSLRA IPWVFSWTQT RFLLPAWYGV GTALKSFVDQ DPVKNMKLLR YFYFKWPFFN
     MVISKVEMTL SKVDLTIASH YVQELSKPED RERFDRLFQQ IKQEYQLTRD FAMEITAHPH
     LLDGDRSLQR SVLLRNRTIV PLGLLQISLL KRLRQVTQEA ETSGVRYRRY SKEELLRGAL
     LTINGIAAGM RNTG
//