ID   CAPP_SYNPW              Reviewed;        1003 AA.
AC   A5GIW5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 81.
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};
GN   OrderedLocusNames=SynWH7803_0454;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000255|HAMAP-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; CT971583; CAK22880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5GIW5; -.
DR   SMR; A5GIW5; -.
DR   STRING; 32051.SynWH7803_0454; -.
DR   KEGG; syx:SynWH7803_0454; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   Proteomes; UP000001566; 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; Reference proteome.
FT   CHAIN           1..1003
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_1000025599"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
FT   ACT_SITE        646
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00595"
SQ   SEQUENCE   1003 AA;  113205 MW;  C6F5581CD6DC2CEE CRC64;
     MIMTVSDPGG SSMSSSSAIT PESEQAMAAV NDAPVGGQLL QQRLALVEDL WQTVLRSECP
     AEQAERLLRM KQLSDPVLPE GNAVSSDALV SLIRDMDLSE AIAAARAFSL YFQLVNILEQ
     RIEEDGYLES IVRSQDTAEQ INPFTPPLAT QTEPATFREL FERLRRLNVP PAQLETLLQE
     LDIRLVFTAH PTEIVRHTVR HKQRRVASLL QQLEAQTESS TFEAGTIRLQ LEEEIRLWWR
     TDELHQFKPS VLDEVDYALH YFQQVLFDAM PQLRRRLSSA LASSYPDVQL PPSSFCTFGS
     WVGSDRDGNP SVTTDITWRT ACYQRQLMLE RYVSAVQGLR DQLSISMQWS QVSAPLLESL
     EMDRLRFPEV YEERATRYRL EPYRLKLSFV LERLRLTQIR NQQLAEAGWR APADGLLSSN
     PEAPQSESLH YGSVAEFRSD LELIRTSLVS TDLTCEPLDT LLTQVHIFGF SLAGLDIRQE
     STRHSDALDE VSRYLNPDQA YGDLNEQERV QWLLQELQTR RPLIPPSVSW SPTTEETVDV
     FRTLHRLQDE FGSRICRTYV ISMSHSVSDL LEVLLLSKEA GLVEPSAGHA DLLVVPLFET
     VEDLQRAPEV MEELFQTPLY RNLLPRVGSQ GQPLQELMLG YSDSNKDSGF LSSNWEIHKA
     QIALQDLAAR NGVALRLFHG RGGSVGRGGG PAYQAILAQP SGTLQGRIKI TEQGEVLASK
     YSLPELALYN LETVSTAVVQ NSLVTNQLDA TPSWNDLMAR LARCSRRHYR ALVHDNPDLV
     AFFEQVTPIE EISKLQISSR PARRKTGTRD LSSLRAIPWV FGWTQSRFLL PSWFGVGTAL
     HEELVNDPDQ MSLLRTLHQR WPFFRMLISK VEMTLSKVDL DLARHYVTSL GSADHRQAFD
     GIYTTIAEEY SLTHRLVLEI TGQERLLDAD PALQLSVDLR NRTIVPLGFL QVALLRRLRD
     QNRQPPMSES PSDGDGRTYS RSELLRGALL TINGIAAGMR NTG
//