ID   CAPP_SYNP6              Reviewed;        1053 AA.
AC   P06516;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
GN   Name=ppc; OrderedLocusNames=syc1846_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2998946; DOI=10.1016/0378-1119(85)90227-6;
RA   Katagiri F., Kodaki T., Fujita N., Izui K., Katsuki H.;
RT   "Nucleotide sequence of the phosphoenolpyruvate carboxylase gene of the
RT   cyanobacterium Anacystis nidulans.";
RL   Gene 38:265-269(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
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; M11198; AAA22052.1; -; Genomic_DNA.
DR   EMBL; AP008231; BAD80036.1; -; Genomic_DNA.
DR   PIR; A24517; QYYC.
DR   AlphaFoldDB; P06516; -.
DR   SMR; P06516; -.
DR   KEGG; syc:syc1846_d; -.
DR   eggNOG; COG2352; Bacteria.
DR   Proteomes; UP000001175; 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; Lyase; Magnesium.
FT   CHAIN           1..1053
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166638"
FT   REGION          461..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        246
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        699
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1053 AA;  121084 MW;  1EDDA7DD8DFFD364 CRC64;
     MLAVSLRDHG FPSATVQIRP AFCVQSDVVG SGNPPRMNYC QNARTAMSAA LQSSDDAFRT
     VSSPLATDLD LSSPLEFFLR HRLTVVEELW EVVLRQECGQ ELVDILTQLR DLTSPEGQAP
     EVGGEALVQV IETLELSDAI RAARAFALYF QLINIVEQHY EQTQYQLAYE RSRLEPLPGP
     DESPEGLHTI EIPQHQLDPF AAVIPLNQDP ATFQTLFPRL RQLNVPPQMI QELTDRLDIR
     LVFTAHPTEI VRHTIRDKQR RIAYLLRQLD ELETGKNRGF RELEAQNIRQ QLTEEIRLWW
     RTDELHQFKP TVLDEVDYAL HYFQEVLFEA IPLLYQRFRL ALQGTFPDLQ PPRYNFCQFG
     SWVGSDRDGN PSVTSAVTWQ TACYQRSLVL DRYITAVEHL RNVLSLSMHW SEVLPELLSS
     LEQESMLFPE TYEQLAVRYR QEPYRLKLSY ILERLHNTRD RNTRLQQQQE KDPTTPLPEY
     RDGTLYQAGT AFLEDLKLIQ HNLKQTGLSC YELEKLICQV EIFGFNLVHL DIRQESSRHS
     DAINEICEYL QILPQPYNEL SEAERTAWLV QELKTRRPLV PARMPFSEST REIIETLRMV
     KQLQEEFGEA ACQTYIISMS RELSDLLEVL LLAKEVGLYD PVTGKSSLQV IPLFETVEDL
     QNAPRVMTAL FELPFYTQLN PTQSEPLQEV MLGYSDSNKD SGFLSSNWEI HKAQKALGTV
     ARDHRVKLRI FHGRGGSVGR GGGPAYEAIL AQPGRTTDGR IKITEQGEVL ASKYALPELA
     LYNLETITTA VIQSSLLGSG FDDIEPWNQI MEELAARSRR HYRALVYEQP DLVDFFNQVT
     PIEEISKLQI SSRPARRKTG KRDLGSLRAI PWVFSWTQSR FLLPSWYGVG TALQEFLQER
     PEQNLNLLRY FYEKWPFFRM VISKVEMTLA KVDLQIAHHY VHELANPEDQ ERFERVFSQI
     AAEFQLTCHL VLTITNHGRL LDGDPELQRS VQLRNGTIVP LGFLQVALLK RLRQYRQQTE
     TTGLMRSRYS KGELLRGALL TINGIAAGMR NTG
//