ID K9YGH5_HALP7 Unreviewed; 1013 AA.
AC K9YGH5;
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 OrderedLocusNames=PCC7418_3855 {ECO:0000313|EMBL:AFZ45959.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ45959.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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,
CC ECO:0000256|HAMAP-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; CP003945; AFZ45959.1; -; Genomic_DNA.
DR AlphaFoldDB; K9YGH5; -.
DR STRING; 65093.PCC7418_3855; -.
DR KEGG; hao:PCC7418_3855; -.
DR PATRIC; fig|65093.3.peg.4069; -.
DR eggNOG; COG2352; Bacteria.
DR HOGENOM; CLU_006557_2_0_3; -.
DR Proteomes; UP000010481; 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:AFZ45959.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010481}.
FT ACT_SITE 196
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10111"
FT ACT_SITE 656
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT ECO:0000256|PROSITE-ProRule:PRU10112"
SQ SEQUENCE 1013 AA; 117004 MW; 612E7661E33602A0 CRC64;
MTSLLQAFSQ DTNNSSRSDT FLTDRIKLIE DLWESVLRAE CGQELVDLLQ QLRSMGSPEG
QATGLPTSSV PQLIEDLPLN DAVRAARAFA LYFQLINIVE QHYEQREQQL NRYFSHDKTE
KDLAEGNIKG QQTETDASHS VLGAQLLEKT WQGNSTYQKA GTFDWLFPYL KKLNVPPQLI
QRLLNQLDIR LVFTAHPTEI VRHTIRKKQR RMSQILQHID QSEIAAQSLG FLESPEAIAA
TEQLKEEIRL WWRTDELHQF KPEVLDEVDY ALHYFQEVLF DTIPHLSSRL KQSLNSSFKD
LNPPQNNFCR FGSWVGADRD GNPSVTPTVT WETACYQRGI VLERYLQSVK RLSTLLSLSL
HWSDVLPELL ESLERDRALM PDVYERLSIR YRREPYRLKL AYIEQRLEHT LQRNHFLSSE
QQAPRETIEK NRQTIYTFGE EFLEELKLIQ RSLTETGLTC RDLEHLICQV EIYGFNLVEL
DMRQESSRHS DTVTEITDYL QLLPQSYNDL SEEERVRWLS EELQTRRPLI PKELPFSEKT
KETVETFRLL KQLQQEFGCE VCQTYIISMS HHVSDILEVL LLAKEAGIYD PATGKCSLQV
VPLFETVDDL LRAPSVMKAL FELPLYRACL AGGYGQENSD EYDIQEVMLG YSDSNKDSGF
LSSNWEIHKA QKALQTLAQG YGVSLRIFHG RGGSVGRGGG PTYEAILAQP SSTINGRIKI
TEQGEVVASK YSLPELALYH LETATTAVIQ ASILGSGFDD INPWQNIMER LAARSRQHYR
ALIYEEPDFL DFFLSVTPIQ EISQLQISSR PARRQGGKKD LSSLRAIPWV FSWTQTRFLL
PAWYGVGTAL QDFLYQDQER SCEQNTKLLR YFYWKWPFFR MVISKVEMTL AKVDLQIAHH
YLKELANPED YERFERIFQQ ISDEYHLTSE LVRLITNHEK LLDGDPDLQR SVQLRNRTIV
PLGFLQVSLI KRLRQYSNES ASEVIHFRYS KEELLRGALL TLNGIAAGMR NTG
//
