ID   K9VB81_9CYAN            Unreviewed;      1041 AA.
AC   K9VB81;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 63.
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=Osc7112_0330 {ECO:0000313|EMBL:AFZ04949.1};
OS   Oscillatoria nigro-viridis PCC 7112.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ04949.1, ECO:0000313|Proteomes:UP000010478};
RN   [1] {ECO:0000313|EMBL:AFZ04949.1, ECO:0000313|Proteomes:UP000010478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ04949.1,
RC   ECO:0000313|Proteomes:UP000010478};
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., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
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; CP003614; AFZ04949.1; -; Genomic_DNA.
DR   RefSeq; WP_015174284.1; NC_019729.1.
DR   AlphaFoldDB; K9VB81; -.
DR   STRING; 179408.Osc7112_0330; -.
DR   KEGG; oni:Osc7112_0330; -.
DR   PATRIC; fig|179408.3.peg.410; -.
DR   eggNOG; COG2352; Bacteria.
DR   HOGENOM; CLU_006557_2_0_3; -.
DR   OrthoDB; 9768133at2; -.
DR   Proteomes; UP000010478; 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:AFZ04949.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010478}.
FT   REGION          131..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        689
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1041 AA;  119124 MW;  624B3A4B5EEA0E63 CRC64;
     MSSVLQSSEQ AIDATSISHS PAYSKSDLFL RNRLKVVEDL WESVLRQECG QELVDLLQQM
     RSVNSAEGQA THFRESNVVQ LIEKLDLNAA IRAARAFALY FQLINIVEQH YEQRDQQLAY
     ASSNDAGGRM FSKLPGQAMD APDRPRHREG PGPAQMALNK ADSSETIARD AGTFHQLFPM
     LLRLNVPSQQ IQRLIDQLDI RLVFTAHPTE IVRHTIRTKQ RRMAKILQQL DQVDEKFQVI
     GAESPSPYPV SCWEAAALQE QLMEEIRLWW RTDELHQFKP TVLDEVEYTL HYFEEVLFDA
     IPELYHRLKQ ALHASYPYLK PPSYNFCKFG SWVGSDRDGN PSVTPKVTWQ TACYQRHLVL
     QKYISAVKRL NELLSLSLHW SDVLPELLES LDRDKSEFPD VYEQWAIRYR QEPYRLKLAY
     VQQRLENTRD RNWRLYKGDE LQREREALSE HPGMTGLYRS GAEFLTELKL IEHNLVETGL
     SCRDLENLIC QVEIYGFNLA YLDIRQESTV HSDALREIAE YLQILPKSYN QMSECDRVIW
     LATELQTRRP LIPAELPFSP KTCETINTFR VLRQMQQEFG PEICQTYVIS MSHDVSDLLA
     VLLLAKEAGL YDPATGISNI QVVPLFETVE DLKKAPEVME KIFDLPLYRA LLAGGYAQEI
     AEKTEENIQC PIENIKLQEV MLGYSDSNKD SGFLSSNWEI HKAQKALQMV AEKHGVELRI
     FHGRGGSVGR GGGPAYKAIL AQPGKSISGR IKITEQGEVL ASKYSLPELA LYNLETVATA
     VIQASLLHTG FDGIDPWNEI MEELSARSRS HYRHLIYEQP DLVDFFHQVT PIQEISQLQI
     SSRPARRGGK KDISGLRAIP WVFSWTQSRF LLPSWYGVGT ALQEFLLEEP EEHMKLLQYF
     YLKWPFFRMV ISKVEMTLSK VDLQIAEHYV RELALPADKE RFQTLFEQIA AEFHLIRGLV
     LTITGHQRLL DEDPSLQRSV QLRNATIVPL GLLQVSLLKR LRQHGSSGIP GVIHSRYSKG
     ELLRGALLTI NGIAAGMRNT G
//