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Database: UniProt/TrEMBL
Entry: K9YGH5_HALP7
LinkDB: K9YGH5_HALP7
Original site: K9YGH5_HALP7 
ID   K9YGH5_HALP7            Unreviewed;      1013 AA.
AC   K9YGH5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   22-NOV-2017, entry version 34.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946768};
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; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; 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.,
RA   Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M.,
RA   Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M.,
RA   Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M.,
RA   Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-
RT   driven genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle. {ECO:0000256|HAMAP-
CC       Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|HAMAP-Rule:MF_00595,
CC       ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00946766};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946753}.
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DR   EMBL; CP003945; AFZ45959.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFZ45959; AFZ45959; PCC7418_3855.
DR   KEGG; hao:PCC7418_3855; -.
DR   PATRIC; fig|65093.3.peg.4069; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
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   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; PTHR30523; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 2.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946757};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010481};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00946754,
KW   ECO:0000313|EMBL:AFZ45959.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:AFZ45959.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010481}.
FT   ACT_SITE    196    196       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    656    656       {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
//
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