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Database: UniProt/TrEMBL
Entry: B6XSJ6_9BIFI
LinkDB: B6XSJ6_9BIFI
Original site: B6XSJ6_9BIFI 
ID   B6XSJ6_9BIFI            Unreviewed;       918 AA.
AC   B6XSJ6;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   05-JUL-2017, entry version 54.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   Name=ppc {ECO:0000313|EMBL:EEB22423.1};
GN   ORFNames=BIFCAT_00056 {ECO:0000313|EMBL:EEB22423.1};
OS   Bifidobacterium catenulatum DSM 16992 = JCM 1194 = LMG 11043.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=566552 {ECO:0000313|EMBL:EEB22423.1, ECO:0000313|Proteomes:UP000003882};
RN   [1] {ECO:0000313|EMBL:EEB22423.1, ECO:0000313|Proteomes:UP000003882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB22423.1,
RC   ECO:0000313|Proteomes:UP000003882};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
RA   Liep D., Gordon J.;
RT   "Draft genome sequence of Bifidobacterium catenulatum (DSM 16992).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB22423.1, ECO:0000313|Proteomes:UP000003882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16992 {ECO:0000313|EMBL:EEB22423.1,
RC   ECO:0000313|Proteomes:UP000003882};
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 (OCT-2008) 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: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}.
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:EEB22423.1}.
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DR   EMBL; ABXY01000001; EEB22423.1; -; Genomic_DNA.
DR   RefSeq; WP_003833568.1; NZ_JDTP01000016.1.
DR   EnsemblBacteria; EEB22423; EEB22423; BIFCAT_00056.
DR   KEGG; bcat:BBCT_0015; -.
DR   PATRIC; fig|566552.18.peg.16; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000003882; 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   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:UP000003882};
KW   Kinase {ECO:0000313|EMBL:EEB22423.1};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169, ECO:0000313|EMBL:EEB22423.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:EEB22423.1};
KW   Transferase {ECO:0000313|EMBL:EEB22423.1}.
FT   ACT_SITE    181    181       {ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    580    580       {ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   918 AA;  102728 MW;  120F40A4D55C8939 CRC64;
     MTTENEQITP ADAAIVSSGT GTKGPEERDL PASLKEEMDL CLQILREVLG EFDEKLLDKF
     DEVREHALNA SAKRFSGILT DTNPNQDDLQ KVVDIIDKTD VHEAQLLARA FTTYFHLANL
     CEENYRVSVL HSREAAVDDT QAVDPVNEMT CAYHQLINEM GPAKAKELLD KLEFHPVFTA
     HPTEARRKAV EGKIRRISQL LATHKLLGGS DKKENSRRLF NEIDALFRTS PIALKKPTPV
     EESETILDIF DNTLFYTIPQ VYRRFDDWVL GDKAGLVPPV CPAFFHPGSW IGSDRDGNPN
     VTAKVSRQVA RKFSDHVLGA LEIETRRVGK NLTMEAETTP PSAELKSLWN HQKEMSERLT
     DKAALISTKE LHRAVMLVMA DRLKATIDRD ADLMYHSCED YIADLKVVQR SLAEANAKRS
     AYGPLQDLIW QAETFGFHMV EMEFRQHSVV HSRALEDIRE HGLHGERGEL QPMTHEVLDT
     FRALGSIQKR NGIKAARRYI ISFTKSAQNI KDVYELNRLA FSHPKDVPTI DVIPLFEQLE
     DLQNSVDVLE EMIKIPEVQA RLKATGGKME VMLGYSDSSK DAGPTSATLA LHSAQERIAK
     WAESHDIDLT LFHGRGGAVG RGGGPANRAV LAQPVGSVKC RFKLTEQGEV IFARYGNPAL
     AIRHVESVAA ATLLQSAPSV EKRNTDMTAK YADMASKLDE 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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