ID   Q2JW30_SYNJA            Unreviewed;       978 AA.
AC   Q2JW30;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
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   ECO:0000313|EMBL:ABC99042.1};
GN   OrderedLocusNames=CYA_0838 {ECO:0000313|EMBL:ABC99042.1};
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS   A-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321327 {ECO:0000313|EMBL:ABC99042.1, ECO:0000313|Proteomes:UP000008818};
RN   [1] {ECO:0000313|EMBL:ABC99042.1, ECO:0000313|Proteomes:UP000008818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABC99042.1,
RC   ECO:0000313|Proteomes:UP000008818};
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA   Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community revealed by
RT   comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000239; ABC99042.1; -; Genomic_DNA.
DR   RefSeq; WP_011429726.1; NC_007775.1.
DR   AlphaFoldDB; Q2JW30; -.
DR   STRING; 321327.CYA_0838; -.
DR   KEGG; cya:CYA_0838; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008818; 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:ABC99042.1}.
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        187
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        629
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   978 AA;  112463 MW;  B1A06E9186474021 CRC64;
     MTSSSHLTTA ERAVGSANGL KEAPPLAERD PLARALAVDE ALDGRNNLLN RRLQMVEELW
     EAVILQECGQ PLVDLLQRLR SMCSPEGQAL EYPIPEVLQI VEHLSLDAAI QTARAFALFF
     QLINIVEQHY ERAEDSDMRM VDSQQRTVRE NEKFERLFPY LRLQGVPPGL LRRLLERLHI
     RLVFTAHPTE IVRHTIREKQ RAFSHLLSQL DWAEQSHPLQ AQMLREQLAE EVLLWWRTDE
     LHQSKPTVLN EVDYTLHYFE EVLFQAIPLL HEYLSRSLKK SFPSVEPPPA GFCNFGSWVG
     GDRDGNPSVT ANVTWQTARY QRNLILGKYI ESVKALTKTL SVSLHWGDVD SQLLDVLEQD
     RRRMPEVYES FSLQYRQEPY RLKLSYIQRR LELTRERNRN LADSACLPVP PPLDNAYANA
     EEFLADLQLI QSSLKNSGLS CRQLDHLICQ VQVFGFHLAH LDIRQDSSYH EAALTEIFEY
     LRILPRPYSE MTEEEKTAFL LRELQTRRPL IPLEAPFSDK AAELIATFRT LRRLQQEFGM
     AMCQTYVISM SRQLSDLLEV LLLAKEVGLY DPISGRGSLA VVPLFETVED LKGAPEVLRQ
     LLEIPFYRQY LAQQENLQEV MLGYSDSNKD AGFLSSNWEI YKAQQRLQAV AESYGVKLQI
     FHGRGGSVGR GGGPAYEAIL AQPGRSVGGR IKITEQGEVL ASKYSLQDLA IFNLETVTSA
     VIQASLLRTY PNDLHEWSRL MESLAERSRQ VYRNLVYEQE GFVEFFHEVT PIEEISQLQI
     SSRPARRSGN SKDIGSLRAI PWVFSWTQSR FLLPAWYGVG TALEEYAAKG EHNLNHLQHL
     YREWPFFRMV ISKVEMTLAK ADLQIARHYV REMSSPERLE RAMELFELIA QEMYRTREMV
     LKITGHKELL ENDPYLKRSV QLRNRSIVPL GFIQVSLLKR LRGKQKSHFH NTQYNRAELL
     RGALLTINGI AAGMRNTG
//