ID   K9UXX5_9CYAN            Unreviewed;      1017 AA.
AC   K9UXX5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
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   ORFNames=Cal6303_1248 {ECO:0000313|EMBL:AFZ00309.1};
OS   Calothrix sp. PCC 6303.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=1170562 {ECO:0000313|EMBL:AFZ00309.1, ECO:0000313|Proteomes:UP000010477};
RN   [1] {ECO:0000313|EMBL:AFZ00309.1, ECO:0000313|Proteomes:UP000010477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6303 {ECO:0000313|EMBL:AFZ00309.1,
RC   ECO:0000313|Proteomes:UP000010477};
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Calothrix sp. PCC 6303.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003610; AFZ00309.1; -; Genomic_DNA.
DR   RefSeq; WP_015196960.1; NC_019751.1.
DR   AlphaFoldDB; K9UXX5; -.
DR   STRING; 1170562.Cal6303_1248; -.
DR   KEGG; calt:Cal6303_1248; -.
DR   PATRIC; fig|1170562.3.peg.1351; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010477; 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:AFZ00309.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010477}.
FT   ACT_SITE        196
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        664
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1017 AA;  116359 MW;  EC77E78DBC7905EF CRC64;
     MGSLIYSFAE AVNIYPASDL FLRHRLQVVE ELWEEVLQQE CGQATVDLLK KLRDLCSPEG
     QATKDQAASV FKLIEQLSIN EAIRAARAFA LYFQLINIIE QDYEQRQQLT RYEAEPENKG
     EEAVTSTVYC QDEESFHHNN GVGAEMLAKS WHNSDNSKHK GTFSGLFPQL FKLNVPPQQI
     QRLISHLDVQ LVFTAHPTEI VRHTIRGKQR QVVQLLQQLD ALEKRAGGSL TGGFLWEAEE
     LQSQLIEEIR LWWRTDELHQ FKPSVLDEVD YALHYFQEVL FDAIPQLYRR FKHTLNQTFP
     WLEPPQKNFC KFGSWVGGDR DGNPSVTPAI TWETACYQRN IVLEKYTKAV KQLIELISVS
     MQWSDVLPDL LESLEMEQAQ MSEVYDQLAL RYRQEPYRLK LSYILKRLEN TSIRNKALQK
     GEILNDEHHH HVYHSGEEFL AELRLIQHNL SETGLTSQQL ENLICQVEIF GFNLTQLDIR
     QESSRHADAL NEVVEYLGIL NKPYNDMSEV ERVAWLTSEL KTRRPLIAAE LPFSEKTNDV
     ISTFRIVRSL QQEFGYNVCQ TYIISMCREV SDVLEVLLFA KEAGLYDPGT AIGTIQVVPL
     FETVEDLLRS RSVMGELFEL PLYRALLAGG YEITENHPNS LSPTSSPLTP NLQEVMLGYS
     DSNKDSGFLS SNWEIHKAQK SLQEIAEGYG ISLRIFHGRG GSVGRGGGPA YEAILAQPGH
     SINGRIKITE QGEVLASKYS LRDLALYNLE TITTAVIQAS LLKTGFDDIE AWNEIMEELA
     ARSRQHYRAL IYEQPDFIDF FHQVTPIEEI SQLQISSRPA RRPSGKKDLT SLRAIPWVFS
     WTQIRVLLPS WYGVGTALQE FLNEEPEEHM KLLRYFYIKW PFFKMVISKA EMTLAKVDLQ
     MASHYVQELS HPEDKPRFDK VFAQIAEEYY LTRNLVLQIT GNKCLLDGDP VLQRSVQLRN
     GTIVPLGFIQ VSLLKRLRQS KNIPTSAVIH SRYSKGELLR GALLTINGIA AGMRNTG
//