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Database: UniProt/TrEMBL
Entry: U5P945_9STRE
LinkDB: U5P945_9STRE
Original site: U5P945_9STRE 
ID   U5P945_9STRE            Unreviewed;       941 AA.
AC   U5P945;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-SEP-2017, entry version 27.
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=N596_04285 {ECO:0000313|EMBL:AGY40020.1};
OS   Streptococcus sp. I-G2.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1156431 {ECO:0000313|EMBL:AGY40020.1, ECO:0000313|Proteomes:UP000017120};
RN   [1] {ECO:0000313|EMBL:AGY40020.1, ECO:0000313|Proteomes:UP000017120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I-G2 {ECO:0000313|EMBL:AGY40020.1,
RC   ECO:0000313|Proteomes:UP000017120};
RA   Hyun D.-W.;
RT   "Genome sequence of Streptococcus sp. IG2 isolated from human ileal
RT   fluid.";
RL   Submitted (SEP-2013) 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, ECO:0000256|SAAS:SAAS00730191}.
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; CP006805; AGY40020.1; -; Genomic_DNA.
DR   RefSeq; WP_023023856.1; NC_022584.1.
DR   EnsemblBacteria; AGY40020; AGY40020; N596_04285.
DR   KEGG; sig:N596_04285; -.
DR   PATRIC; fig|1156431.3.peg.835; -.
DR   KO; K01595; -.
DR   Proteomes; UP000017120; 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; 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:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017120};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00595,
KW   ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AGY40020.1}.
FT   ACT_SITE    138    138       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    604    604       {ECO:0000256|HAMAP-Rule:MF_00595,
FT                                ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   941 AA;  108067 MW;  DD9E08B3A13A9DCE CRC64;
     MTLQKLESYT NKEIIKEEVE ILTTILEDIA KNLVSPETFD KILELKKLSV SKDYLKLDQI
     VRELSNEEMI VISRYFAILP LLINISEDVD LAFEINHQNN VGQDYLGKLS STIRQVAETE
     NAQEILERLN VVPVLTAHPT QVQRKTMLDL TTQIHSLLRQ HRDVKAGLMN ETKWYNNLRR
     NIEIMMQTDM IREKKLKVTN EITNVMEYYN SSFLQAVPNL MLEYKRLAKE QGIELQQPKP
     ITMGMWIGGD RDGNPFVTAE TLKRSATIQS EVILNYYIQK ISSLYRNFSL STNLSKTSQA
     VEEMAARSSD TSVFREKEPY RRAFHYIQSK LVQTLLNIKE WSVVGSTVDE RHPIERLLGA
     HTHQQGVVSD YIGTRISGAI QELAEDRPPY YETVEEFKQD LTLIQESLIE NKAEALISGE
     FAELLEAVEV FGFFLASIDM RQDSSVHEAC VAELLKEAGI NDHYSDLSED EKCELLLQEL
     LEDPRILSAT HAEKSELLEK ELAIFQTARE LKDRLGEDVI RQTIISHATS VSDMLELAIM
     LKEVGLIDKE SARVQIVPLF ETIEDLDQSE DTMRKYLSLP IAKRWIASKN NYQEIMLGYS
     DSNKDGGYLS SCWTLYKAQQ QLTAIGDEFG VKITFFHGRG GTVGRGGGPT YEAITSQPLR
     SINDRIRLTE QGEVIGNKYG NKDAAYYNLE MLVSATINRM IAKKKSEKSM SDQYNEIMDQ
     IVNRSYDIYR ELVFGNEHFY DYFFESSPIK AISSFNIGSR PAARKTIKEI GGLRAIPWVF
     SWSQSRVMFP GWYGVGSSFK EFIDADPENI ETLRYMYQKW PFFKSLLSNV DMVLSKANMN
     IAFEYAKLCE EEEVRDIFNI ILDEWQLTKD VILQIEGHDE LLAENPYLKD SLDYRMPYFN
     VLNYIQLELI KRQRRGELPA DQDKLIHITI NGVATGLRNS G
//
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