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Database: UniProt/TrEMBL
Entry: A9BCR4_PROM4
LinkDB: A9BCR4_PROM4
Original site: A9BCR4_PROM4 
ID   A9BCR4_PROM4            Unreviewed;      1007 AA.
AC   A9BCR4;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-SEP-2017, entry version 71.
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   ECO:0000313|EMBL:ABX09626.1};
GN   OrderedLocusNames=P9211_16951 {ECO:0000313|EMBL:ABX09626.1};
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059 {ECO:0000313|EMBL:ABX09626.1, ECO:0000313|Proteomes:UP000000788};
RN   [1] {ECO:0000313|EMBL:ABX09626.1, ECO:0000313|Proteomes:UP000000788}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211 {ECO:0000313|Proteomes:UP000000788};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000878; ABX09626.1; -; Genomic_DNA.
DR   ProteinModelPortal; A9BCR4; -.
DR   STRING; 93059.P9211_16951; -.
DR   EnsemblBacteria; ABX09626; ABX09626; P9211_16951.
DR   KEGG; pmj:P9211_16951; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000000788; 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:UP000000788};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:ABX09626.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ABX09626.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000788}.
FT   ACT_SITE    192    192       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    648    648       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   1007 AA;  115065 MW;  AA05EB93777E945A CRC64;
     MIMSKSELGN TPLEQSSDLH SSFRNNQAST TKNSGSLLQQ RLALVEDLWE TVLCSECPSD
     QINRVLRLKK LSNPNNFAGE EEQKNPFNEI VLLIEEMDLA ESIAAARAFS LYFQLVNILE
     QRIEEDTYLE TIGRIEEDAS NQFDPFAPPL ASQTAPATFS QLFERLKRLN VPPGQLEALM
     QEIDIRLVFT AHPTEIVRHT VRHKQRRVAN LLQQFHSEAA ISFSQKESLR QQLEEEIRLW
     WRTDELHQFK PTVLDEVDYA LHYFQQVLFD AMPQLRRRIN AALVKSYPDV EVPRESFCTF
     GSWVGSDRDG NPSVTPEITW RAACYQRQLM LERYINSVQD LRDQLSISMQ WSQVGSQLLE
     SLEMDRVQFP EVYEERAARY RLEPYRLKIS YILQRLKLTH QRNQELAAAG WKIVPEAMNS
     LITSGKPFED LYYCSIAEFR SDLELIRNSL VATDLSCESL DTLLTQVHIF GFSLASLDIR
     QESNRHSDAI DEVTRFIDLP VIYSEMDEKE KVQWLMQELE TRRPLIPSSV DWSPSTQETI
     SVFQMLHRLQ EEFGSRICRS YVISMSHSVS DLLEVLLLAK EAGLVDISSG SADLLVVPLF
     ETVEDLQRAP SVMEELFSSS FYLNLLPRVG EKLQPLQELM LGYSDSNKDS GFLSSNWEIH
     QAQIALQNLA SSHGVALRLF HGRGGSVGRG GGPAYQAILA QPSGTLKGRI KITEQGEVLA
     SKYSLPELAM YNLETVTTAV LQNSLVTNQL DATPSWNELM TRLAARSRRH YRSLVHDNPD
     LVPFFQEVTP IEEISKLQIS SRPTRRKSGS KDLSSLRAIP WVFGWTQSRF LLPSWFGVGH
     ALFIELEEDP AQIELLKMLH QRWPFFRMLI SKVEMTLSKV DLEVANHYVT SLGSRQNKEA
     FNKIFEVISD EYHLTKRLVL RITGKSKLLS ADPALQASVE LRNRTIVPLG FLQVALLRRL
     RDQKRQPPVS EELFNERDLA RTYSRSELLR GALLTINGIA AGMRNTG
//
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