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Database: UniProt/TrEMBL
Entry: C0BUD1_9BIFI
LinkDB: C0BUD1_9BIFI
Original site: C0BUD1_9BIFI 
ID   C0BUD1_9BIFI            Unreviewed;       918 AA.
AC   C0BUD1;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   20-DEC-2017, entry version 54.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00946768};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00946768};
GN   Name=ppc {ECO:0000313|EMBL:EEG70272.1};
GN   ORFNames=BIFPSEUDO_04016 {ECO:0000313|EMBL:EEG70272.1};
OS   Bifidobacterium pseudocatenulatum DSM 20438 = JCM 1200 = LMG 10505.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=547043 {ECO:0000313|EMBL:EEG70272.1, ECO:0000313|Proteomes:UP000003875};
RN   [1] {ECO:0000313|EMBL:EEG70272.1, ECO:0000313|Proteomes:UP000003875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG70272.1,
RC   ECO:0000313|Proteomes:UP000003875};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
RA   Liep D., Gordon J.;
RT   "Draft genome sequence of Bifidobacterium pseudocatenulatum (DSM
RT   20438).";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEG70272.1, ECO:0000313|Proteomes:UP000003875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG70272.1,
RC   ECO:0000313|Proteomes:UP000003875};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid
CC       source for the tricarboxylic acid cycle.
CC       {ECO:0000256|SAAS:SAAS00946761}.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-). {ECO:0000256|SAAS:SAAS00946751}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00946766};
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|SAAS:SAAS00946753}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEG70272.1}.
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DR   EMBL; ABXX02000004; EEG70272.1; -; Genomic_DNA.
DR   RefSeq; WP_004222809.1; NZ_JGZF01000004.1.
DR   STRING; 547043.BIFPSEUDO_04016; -.
DR   EnsemblBacteria; EEG70272; EEG70272; BIFPSEUDO_04016.
DR   KEGG; bpsc:BBPC_0015; -.
DR   PATRIC; fig|547043.19.peg.16; -.
DR   eggNOG; ENOG4105CCA; Bacteria.
DR   eggNOG; COG2352; LUCA.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000003875; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR30523; PTHR30523; 2.
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:SAAS00946757};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003875};
KW   Kinase {ECO:0000313|EMBL:EEG70272.1};
KW   Lyase {ECO:0000256|SAAS:SAAS00946754, ECO:0000313|EMBL:EEG70272.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00946750};
KW   Pyruvate {ECO:0000313|EMBL:EEG70272.1};
KW   Transferase {ECO:0000313|EMBL:EEG70272.1}.
FT   COILED      398    418       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    181    181       {ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    580    580       {ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   918 AA;  102765 MW;  629D041DC80DA48C CRC64;
     MTIENEQITP ADAAIVSSGT GTKGPEERDL PASLKEEMDL CLQILREVLG EFDEKLLAKF
     DEVREHALNA SAERFSGILT DTNPNQDDLQ KVVDIIDKTD VHEAQLLARA FTTYFHLANL
     CEENYRVSVL HSREAAVDDT QAVDPVNEMT CAYHQLINEM GPAKAKELLD QLEFHPVFTA
     HPTEARRKAV EGKIRRISQL LATHKLLGGS DKKENSRRLF NEIDALFRTS PIALKKPTPV
     EESETILDIF DNTLFYTIPQ VYRRFDDWIL GDKAGLVPPV CPAFFHPGSW IGSDRDGNPN
     VTAKVSRQVA RKFSDHVLGA LQIETRRVGK NLTMEAETTP PSAELKSLWN HQKEMSERLT
     DKAALISTKE LHRAVMLVMA DRLKATIDRD ADLMYHSCED YIADLKVVQR SLAEANAKRS
     AYGPLQDLIW QAETFGFHMV EMEFRQHSVV HSRALEDIRE HGLHGERGEL QPMTHEVLDT
     FRALGSIQKR NGIKAARRYI ISFTKSAQNI RDVYELNRLA FSHPKDVPTI DVIPLFEQLE
     DLQNSVDVLE EMIKIPEVQA RLKATGGKME VMLGYSDSSK DAGPTSATLA LHSAQERIAK
     WAESHDIDLT LFHGRGGAVG RGGGPANRAV LAQPVGSVKC RFKLTEQGEV IFARYGNPAL
     AIRHVESVAA ATLLQSAPSV EKRNTDMTAK YADMANKLDE AAHNRFLDLL NTDGFAPWFS
     TVTPLTEIGL LPIGSRPAKR GLGAKSLDDL RTIPWIFSWA QARINLAAWY GLGTACEQFG
     DLNTLRQAYE EWPLFSTFID NIEMSLAKTD ERIAKMYLAL GDREDLNKKV LDEMELTRKW
     VLEIVGDKWP LQHRHVLGQA IRIRSPYVDA LSATQVLALG SLRKRVDKEE LTHGQKENYT
     YLILCTVSGV AAGLQNTG
//
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