ID   K9UQ46_CHAP6            Unreviewed;      1008 AA.
AC   K9UQ46;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Cha6605_5443 {ECO:0000313|EMBL:AFY96329.1};
OS   Chamaesiphon minutus (strain ATCC 27169 / PCC 6605).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Chamaesiphonaceae;
OC   Chamaesiphon.
OX   NCBI_TaxID=1173020 {ECO:0000313|EMBL:AFY96329.1, ECO:0000313|Proteomes:UP000010366};
RN   [1] {ECO:0000313|EMBL:AFY96329.1, ECO:0000313|Proteomes:UP000010366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27169 / PCC 6605 {ECO:0000313|Proteomes:UP000010366};
RG   US DOE Joint Genome Institute;
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 Chamaesiphon sp. PCC 6605.";
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; CP003600; AFY96329.1; -; Genomic_DNA.
DR   RefSeq; WP_015162412.1; NC_019697.1.
DR   AlphaFoldDB; K9UQ46; -.
DR   STRING; 1173020.Cha6605_5443; -.
DR   KEGG; cmp:Cha6605_5443; -.
DR   PATRIC; fig|1173020.3.peg.6252; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010366; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:AFY96329.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010366}.
FT   COILED          203..230
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        659
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1008 AA;  115110 MW;  B98B8284E9567C51 CRC64;
     MQPLTHMLEP ELMVSTPSNL LLNHRLKVIE DLWERVLRDA CGQELVNLLN QLREMCSSDG
     SAAEPLPQAV HVLIEKLDLK DAIRAARAFA LYFQLINIVE QHYEQCEQKL ALKLSLQYSV
     PIHAAPQTDR ASEHVAPLGA GLLEKTWQAS SVEQQKDRGT FAALFPLLKA AGVPPQQVQR
     LFDELDIGLV FTAHPTEIVR HTIRDKQRRV AQILEKLDRA EEDMTRLGIQ SSWEVAELEG
     QLLEEILLWW RTDELHQFKP TVLDEVDYTL HYFEEVLFDA IPQLSQRLNL ALKQSFPYLT
     PPSNRFCRFG SWVGSDRDGN PSVTPKVTWQ TACYQRGIVL KKYIKCTRAL TNALSLSLHW
     SNVLPELLES LEQDKSHFPE IYEDWAIRYR QEPYRLKLTY IIKRLSNTLD RSRQVSDWDS
     LQFPKADLNP NTCYHSGADF LKELRLIRQS LQQTGLTCQA LETLICQVEI YGFNLAQLDI
     RQESGRHADT IAEITEYLQV FPKSYHDLSE TERVEWLVGE LKTRRPLIPG ELPFSPKAVE
     TIETFRMLRR LHQEFGPEIC QTYVISMNRD VSDILEVMLL GKESGLYDPA TGITSLQVVP
     LFETVEDLKK APLVMQSLFE LPLYRAALTG GYQPTPANAI PGLVPHLQEV MLGYSDSNKD
     AGFLSSNWEI HKAQKALQAI AEKFNVKLRI FHGRGGSVGR GGGPSHEAIL AQPGQSINGR
     IKITEQGEVL ASKYSLPELA LYNLEQVASA VIKTSLMSGG VDDIEPWNEV MEDLADRSRR
     HYRALVYDRP ELVNFFHQVT PIDEISHLQI SSRPARRGGK RDLASLRAIP WVFSWTQSRF
     LLPSWYGVGT ALEEFVAECP QENFELLQGF YRKWPFFRMA ISKVEMTISK VDLQIARHYM
     EELSQPEDRE QFEILFERIA HEYRLVSDLV LRISGHERFL DDNPELQRSI QLRNGSIVPL
     GFLQVSLLKR LRQHGGAGMI YSRYSKRELL DGALLTINGI AAGMRNTG
//