ID   E0UJ33_GLOV7            Unreviewed;      1020 AA.
AC   E0UJ33;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
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   OrderedLocusNames=Cyan7822_2645 {ECO:0000313|EMBL:ADN14613.1};
OS   Gloeothece verrucosa (strain PCC 7822) (Cyanothece sp. (strain PCC 7822)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Gloeothece; Gloeothece verrucosa.
OX   NCBI_TaxID=497965 {ECO:0000313|EMBL:ADN14613.1, ECO:0000313|Proteomes:UP000008206};
RN   [1] {ECO:0000313|Proteomes:UP000008206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7822 {ECO:0000313|Proteomes:UP000008206};
RX   PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP002198; ADN14613.1; -; Genomic_DNA.
DR   RefSeq; WP_013322718.1; NC_014501.1.
DR   AlphaFoldDB; E0UJ33; -.
DR   STRING; 497965.Cyan7822_2645; -.
DR   KEGG; cyj:Cyan7822_2645; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000008206; 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:ADN14613.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008206}.
FT   ACT_SITE        194
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        667
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1020 AA;  117813 MW;  EFEE01813F552FAB CRC64;
     MSSLVQVPTT PLQFFSTSDL FLQARLKLVE DLWEAVLKAE CGQDLVDLLI KLRAICSEQG
     QAQKALEDSI TQLIEKLDLN EAVRTSRAFA LYFQLINIVE QHYEQRDQQL SRRATYNEGE
     SSAKNGINGE QTSIFSSAFG ANWLERSLND EKQNDQKIGT FHWLFPYLKQ LNVPPQQIQR
     LLEQLDVRLV FTAHPTEIVR HTIRRKQRRI AHILQKLDQA EETFRGMGLT NSWEAEEAKE
     QLKEEIRLWW RTDELHQFKP TVLDEVDYSL HYFNEVLFEA IPQLALRLKR TLKSAFPRLR
     PPKNNFCYFG SWVGGDRDGN PFVTPEVTWA TACYQRNVVI EKYIERVDEL SNILSPSLHW
     CNVLPDLLDS LEKDRVQIPQ VYNQLAIRYR QEPYRLKLAY IKKRLENTRD RNSRLANPEE
     RLLVFKTTNA NNYQNKEEFI EELKLMRRNL ESTGLSCQEL DSLICQVEVY GFNLTQLDFR
     QESSNHSDAI NEIAEYLQIL PKPYNQLTEA ERTAWLIEEL KTRRPLIPQE MPFSEKTCEV
     IETLRMLRQL QQEFGLEICH TYIISMTNEV SDVLEVLLLA QEAGLYDPAT CSSTIRIVPL
     FETVEDLKRA PEIMRALFEL TLYRATLAGG YDHLASLQGE NVGELKPPLL EPTNLQEIMV
     GYSDSNKDSG FLSSNWEIHK AQKALQKVAK RYGLDLRLFH GRGGSVGRGG GPAYAAILAQ
     PTATVNGRIK ITEQGEVLAS KYSLPELALY NLETIVTAVI QSSLLGCGFD DIQVWNEIME
     ELASCSRKAY RALIYEEPDF VDFFMSVTPI QEISQLQISS RPARRKSGKK DLSTLRAIPW
     VFSWTQTRFL LPAWYGVGTA LEQFISTEPE EHLKLLRYFY LKWPFFKMVI SKVEMTLSKV
     DLQIAYHYVK ELSQPEDRER FERLFEQIAQ EYHRTCRLVL EITENKRLLD GDPTLQRSVQ
     LRNGTIVPLG FLQVSLIKRL RQYNAQAESG VINFRYSKEE LLRGALLTIN GIAAGMRNTG
//