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Database: UniProt/TrEMBL
Entry: Q46IP1_PROMT
LinkDB: Q46IP1_PROMT
Original site: Q46IP1_PROMT 
ID   Q46IP1_PROMT            Unreviewed;       994 AA.
AC   Q46IP1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-SEP-2017, entry version 87.
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   OrderedLocusNames=PMN2A_1147 {ECO:0000313|EMBL:AAZ58637.1};
OS   Prochlorococcus marinus (strain NATL2A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59920 {ECO:0000313|EMBL:AAZ58637.1, ECO:0000313|Proteomes:UP000002535};
RN   [1] {ECO:0000313|EMBL:AAZ58637.1, ECO:0000313|Proteomes:UP000002535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL2A {ECO:0000313|EMBL:AAZ58637.1,
RC   ECO:0000313|Proteomes:UP000002535};
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; CP000095; AAZ58637.1; -; Genomic_DNA.
DR   RefSeq; WP_011295491.1; NC_007335.2.
DR   EnsemblBacteria; AAZ58637; AAZ58637; PMN2A_1147.
DR   KEGG; pmn:PMN2A_1147; -.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   OrthoDB; POG091H040O; -.
DR   PhylomeDB; Q46IP1; -.
DR   Proteomes; UP000002535; 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:UP000002535};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595, ECO:0000256|SAAS:SAAS00635169,
KW   ECO:0000313|EMBL:AAZ58637.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AAZ58637.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002535}.
FT   ACT_SITE    178    178       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    634    634       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   994 AA;  113292 MW;  30DFA0C823B3A0CE CRC64;
     MLKNPSNENI SNHSTVCVED QDPGSLLQQR LELVEDLWKT VLKSECPPDQ TERLLRLKQL
     SDPSKSNQDN SSKAIVQLIT KMDLAEAISA ARAFSLYFQL VNILEQRIEE DSYLESIEKG
     KLDTSNYKID PFAPALASQT APATFTQLFE RLRRLNVPPA QLDGLMREMD IRLVFTAHPT
     EIVRHTVRHK QRRVATLLQQ LQSNSLISES EKEIFRLQLE EEIRLWWRTD ELHQFKPTVL
     DEVDYALHYF QQVLFDAMPQ LRRRLTTALA SSYPDVEIPN EAFCTFGSWV GSDRDGNPSV
     TPEITWRTAC YQRQLMLDRY IASVQDLRDQ LSISMQWSQV SSPLLESLEM DRVRFPEVYE
     ERAARYRLEP YRLKLSYTLE RLRLTQLRNK QLADAGWQFS PDGKPLISTN NSFDEVLHYK
     SVEELKNELE LIRNSLVSTD LTCEPLDTLL NQVHIFGFSL ASLDIRQEST RHSDALDELT
     RYLDLPESYG VMSEESRVQW LMKELRTRRP LIPPSFEWSK STQETISVFH MLHRLQKEFG
     TRICRSYVIS MSHTASDLLE VLLLAKESGL IDPTLGASDL LVVPLFETVE DLQHAPSVME
     SLLQTDVYRE LLPRVGEKKQ PLQELMLGYS DSNKDSGFLS SNWEIHKAQI ALQDLASRQG
     IALRIFHGRG GSVGRGGGPA YQAILAQPSG TLQGRIKITE QGEVLASKYS LPELALYNLE
     TVTTAVIQNS LVTNKLDATP SWNELMTRLA ARSREHYRAL VHDNPDLVQF FQVVTPIEEI
     SKLQISSRPA RRKSGAKDLS SLRAIPWVFG WTQSRFLLPS WFGVGTALAT ELKADPDQME
     MLRMLNQRWP FFRMLISKVE MTLSKVDLDV AHHYVVSLGG SDDRDAFARI FDIISSEYSL
     TKKLILEITG KSKLLSADPA LQLSVNLRNR TIVPLGFLQV ALLKRLRDQN RQPPISEDVS
     IDSTQSSRTY SRSELLRGAL LTINGIAAGM RNTG
//
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