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Database: UniProt/TrEMBL
Entry: A0A089PAW5_9PROC
LinkDB: A0A089PAW5_9PROC
Original site: A0A089PAW5_9PROC 
ID   A0A089PAW5_9PROC        Unreviewed;       978 AA.
AC   A0A089PAW5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-SEP-2017, entry version 19.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635171};
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:SAAS00635171};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=EW14_1933 {ECO:0000313|EMBL:AIQ95940.1};
OS   Prochlorococcus sp. MIT 0604.
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=1501268 {ECO:0000313|EMBL:AIQ95940.1, ECO:0000313|Proteomes:UP000029517};
RN   [1] {ECO:0000313|EMBL:AIQ95940.1, ECO:0000313|Proteomes:UP000029517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 0604 {ECO:0000313|EMBL:AIQ95940.1,
RC   ECO:0000313|Proteomes:UP000029517};
RA   Biller S., Berube P., Thompson J., Kelly L., Roggensack S., Awad L.,
RA   Roache-Johnson K., Ding H., Giovannoni S.J., Moore L.R.,
RA   Chisholm S.W.;
RT   "Genomes of diverse isolates of the marine cyanobacterium
RT   Prochlorococcus.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00595, ECO:0000256|SAAS:SAAS00635164};
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:SAAS00635168}.
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DR   EMBL; CP007753; AIQ95940.1; -; Genomic_DNA.
DR   EnsemblBacteria; AIQ95940; AIQ95940; EW14_1933.
DR   KEGG; prc:EW14_1933; -.
DR   KO; K01595; -.
DR   Proteomes; UP000029517; 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   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; SSF51621; 1.
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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029517};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AIQ95940.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AIQ95940.1}.
FT   ACT_SITE    164    164       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    619    619       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   978 AA;  113006 MW;  F0E9A98B4D2D485E CRC64;
     MDLISNNDPL DKNRLLIEDL WESVLREECP DDQAERLIQL KELSYSKQID GNSSKTSKNE
     IVEIVNSMDL SESIAAARAF SLYFQLVNIL EQRVEEDRYI QSFTNKDVQK SPDNLDPFAP
     ALARQNAPVT FRELFYRLRK LNVPPGKLEE LLQEMDIRLV FTAHPTEIVR HTIRHKQTRV
     ANLLKKIQIE QFLTKEEKNS LKTQLKEEVR LWWRTDELHQ FKPSVLDEVD YALHYFQQVL
     FNAMPQLRCR IAEALTENYP DVQMPSESFC NFGSWVGSDR DGNPSVTPDI TWRTACYQRQ
     LMLERYIIAI SNLRDQLSVS MQWSQVSSSL LESLETDRVK FPEIYEARAT RYRSEPYRLK
     LSYILEKLRL TQERNNLLAD SGWKFDLEGE IDNKNLEKVE NLYYQSVNEF TYDLELIKNS
     LISTDLNCES VNTLLTQVHI FGFSLASLDI RQESTRHSEA IQELTNYLDL SVHYDQMSEE
     EKIKWLIEEL NTKRPLIPSD VNWTNTTEET FAVFKMVKRL QQEFGSRICH SYVISMSHSA
     SDLLEVLLLA KEMGLFDQNS QKSKLLVVPL FETVEDLKRA PEVMEKLFKL DFYRSLLPKV
     GESSKPLQEL MLGYSDSNKD SGFVSSNWEI HRAQISLQNL SSRNNILLRL FHGRGGSVGR
     GGGPAYQAIL AQPSGTLKGR IKITEQGEVL ASKYSLPELA LYNLETVTTA VIQNSLVNNR
     LDATPEWNQL MSRLAETSRS HYRRLVHENP DLLNFFQEVT PIEEISKLQI SSRPARRKKG
     AKDLSSLRAI PWVFGWTQSR FLLPSWFGVG TALSSELNSD PKQIELLRVL HQRWPFFRML
     ISKVEMTLSK VDLEVARYYV DTLGSKENKD SFDDIFEVIS KEYILTKSLI LEITGKNKLL
     ESDRDLKSSV SLRNKTIIPL GFLQVSLLRR LRDQTRQPPI SEFIIDQDES RRAYSRSELL
     RGALLTINGI AAGMRNTG
//
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