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Database: UniProt/TrEMBL
Entry: D2Q6J8_BIFDB
LinkDB: D2Q6J8_BIFDB
Original site: D2Q6J8_BIFDB 
ID   D2Q6J8_BIFDB            Unreviewed;       918 AA.
AC   D2Q6J8;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   05-JUL-2017, entry version 55.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   OrderedLocusNames=BDP_0023 {ECO:0000313|EMBL:ADB08720.1};
OS   Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 /
OS   Bd1).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB08720.1, ECO:0000313|Proteomes:UP000008693};
RN   [1] {ECO:0000313|EMBL:ADB08720.1, ECO:0000313|Proteomes:UP000008693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1
RC   {ECO:0000313|Proteomes:UP000008693};
RX   PubMed=20041198; DOI=10.1371/journal.pgen.1000785;
RA   Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V.,
RA   Bottacini F., Canchaya C., Claesson M.J., He F., Mantzourani M.,
RA   Mulas L., Ferrarini A., Gao B., Delledonne M., Henrissat B.,
RA   Coutinho P., Oggioni M., Gupta R.S., Zhang Z., Beighton D.,
RA   Fitzgerald G.F., O'Toole P.W., van Sinderen D.;
RT   "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic
RT   adaptation to the human oral cavity.";
RL   PLoS Genet. 5:E1000785-E1000785(2009).
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00730191}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00635165}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00635164};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00635168}.
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DR   EMBL; CP001750; ADB08720.1; -; Genomic_DNA.
DR   RefSeq; WP_003838081.1; NC_013714.1.
DR   ProteinModelPortal; D2Q6J8; -.
DR   SMR; D2Q6J8; -.
DR   STRING; 401473.BDP_0023; -.
DR   EnsemblBacteria; ADB08720; ADB08720; BDP_0023.
DR   GeneID; 31605262; -.
DR   KEGG; bde:BDP_0023; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238647; -.
DR   KO; K01595; -.
DR   OMA; PWVFGWT; -.
DR   Proteomes; UP000008693; Chromosome.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR021135; PEP_COase.
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; 2.
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|SAAS:SAAS00635173};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008693};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169, ECO:0000313|EMBL:ADB08720.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:ADB08720.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008693}.
FT   ACT_SITE    181    181       {ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    580    580       {ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   918 AA;  102758 MW;  4697F0908EB45C35 CRC64;
     MTTNDQQITP ADAAIVSSGT GTKGPEERDL PASLKEEMDL CLQILREVLG EFDEQLLASF
     DEVRGYALNA SAERFAGILT DTNPDQDDLQ NVVNTVDKLD MHDAQLLARA FATYFHLANL
     CEENYRVSVL HKRETAVDEN QAVDPVNEMT GAYHQLINEL GPAKARDLLD KLEFHPVFTA
     HPTEARRKAV EGKIRRISRL LEAHKLLGGS DKKENSRRLF NEIDALFRTS PIALKKPTPV
     EEADTILDIF DNTLFYTIPQ VYRRFDDWVL GDKAGLVPPM CPAFFHPGSW IGSDRDGNPN
     VTAKVSRQVA RKFSDHVLGA LEIETRTVGK NLTMEAGTTP PSDELKSLWN HQKEMSERLT
     DKAALISTKE MHRAVMLVMA DRLHYTIERD ADLMYHSCDE FLEDLKIVQR SLAAANAKRS
     AYGPVQDLIW QTETFGFHMV EMEFRQHSVV HSRALEDIRE HGLHGERGPL QPMTHEVLDT
     FRALGAIQKR NGIKAARRYI ISFTKSAQNI KDVYELNRLA FSHPEDVPTI DVIPLFEQLE
     DLQNSVDVLE DMIKIPEVQA RLKATGGKLE VMLGYSDSSK DAGPTSATLA LHSAQERIAK
     WAESHDIDLT LFHGRGGAVG RGGGPANRAV LAQPVGSVKC RFKLTEQGEV IFARYGNPAL
     AIRHVESVAA ATLLQSAPSV EKRNTDMTEK YADMANKLDE AAHNRFLDLL NTPDFAPWFS
     TVTPLTEIGL LPIGSRPAKR GLGAKSLDDL RTIPWIFSWA QARINLAAWY GLGTACEQFG
     DLKTLRQAYE EWPLFSTFID NIEMSLAKTD ERIAKMYLAL GDREDLNKKV LDEMELTREW
     VLKIVGDEWP LQHRHVLGQA IRIRSPYVDA LSVTQVLALG SLRKQVDKEE LTHGQQENYT
     YLILCTVSGV AAGLQNTG
//
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