ID   Q2JKJ2_SYNJB            Unreviewed;       978 AA.
AC   Q2JKJ2;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 110.
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:ABD02797.1};
GN   OrderedLocusNames=CYB_1842 {ECO:0000313|EMBL:ABD02797.1};
OS   Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS   Yellowstone B-Prime).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD02797.1, ECO:0000313|Proteomes:UP000001938};
RN   [1] {ECO:0000313|EMBL:ABD02797.1, ECO:0000313|Proteomes:UP000001938}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
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; CP000240; ABD02797.1; -; Genomic_DNA.
DR   RefSeq; WP_011433437.1; NC_007776.1.
DR   AlphaFoldDB; Q2JKJ2; -.
DR   STRING; 321332.CYB_1842; -.
DR   KEGG; cyb:CYB_1842; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000001938; 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:ABD02797.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001938}.
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;  112660 MW;  1C48A452823D584D CRC64;
     MTSSPHLTAA EGAAGSANGL KEASLFGERD PLAHSLQVNE AFNRRNNLLN RRLQLVEELW
     ESVILQECGQ SLVDLLQRLR SMCSPEGQAL EYPIPEVLQI IEYLSLDATI QTARAFALFF
     QLINIVEQHY ERAEDSDMRM VDSQQRTVRE NEKFERLFPY LRAQGVPPGL LRRLLEQLHI
     RMVFTAHPTE IVRHTIREKQ RAFSRLLSQL DWAEQTQPLQ AQMIKEQMAE EVLLWWRTDE
     LHQSKPTVLN EVDYTLHYFE EVLFQAIPLL HEYLSRSLKK AFPSVEPPPA GFCNFGSWVG
     GDRDGNPSVT ADVTWQTARY QRNLILGKYI ESVKALTKTL SISLHWGDVD SQLLDALEQD
     HRLMPEVYES FSLQYRQEPY RLKLSYIQRR LELTRERNRN LADSACLPTP PPVDNAYANA
     EEFLADLQLI QKSLKNSGLS CRQLDHLIQQ VQVFGFHLAH LDIRQDSSYH EAALTEIFEY
     LRILPRPYNE MTEEEKTAFL LQELQTRRPL IPLEIAFSEK TAELIATFRT LRRLQQEFGL
     AICQTYVISM SRQLSDLLEV LLMAKEVGLY DPISGRGSLA VVPLFETVED LKRAPEVLRQ
     LLEIPFYRQY LAQQGNLQEV MLGYSDSNKD SGFLSSNWEI YKAQQRLQTV AESYGVKLQI
     FHGRGGSVGR GGGPAYEAIL AQPGRSVGGR IKITEQGEVL ASKYSLQDLA IFNLETVTSA
     VIQASLLRTY PNDLHEWSRL MESLAERSRQ VYRNLVYEQE GFVEFFHEVT PIEEISQLQI
     SSRPARRSGS QKDIGSLRAI PWVFSWTQSR FLLPAWYGVG TALQEYVARG EHNLNHLQHL
     YREWPFFRMV ISKVEMTLAK VDLQIARHYV REMSSPERLE RAMELFECIA QEMHRTRTIV
     LQITGHRELL ENDPYLKRSV QLRNRSIVPL GFIQVSLLKR LRERQGSRTG RTRYDRAELL
     RGALLTINGI AAGMRNTG
//