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Database: UniProt/TrEMBL
Entry: D4BLI9_BIFBR
LinkDB: D4BLI9_BIFBR
Original site: D4BLI9_BIFBR 
ID   D4BLI9_BIFBR            Unreviewed;       917 AA.
AC   D4BLI9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   07-JUN-2017, entry version 44.
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:EFE90177.1};
GN   ORFNames=BIFBRE_02924 {ECO:0000313|EMBL:EFE90177.1};
OS   Bifidobacterium breve DSM 20213 = JCM 1192.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=518634 {ECO:0000313|EMBL:EFE90177.1, ECO:0000313|Proteomes:UP000003191};
RN   [1] {ECO:0000313|EMBL:EFE90177.1, ECO:0000313|Proteomes:UP000003191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20213 {ECO:0000313|EMBL:EFE90177.1,
RC   ECO:0000313|Proteomes:UP000003191};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2010) 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:EFE90177.1}.
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DR   EMBL; ACCG02000002; EFE90177.1; -; Genomic_DNA.
DR   RefSeq; WP_003827906.1; NZ_JDUD01000007.1.
DR   EnsemblBacteria; EFE90177; EFE90177; BIFBRE_02924.
DR   GeneID; 29240642; -.
DR   KEGG; bbrd:BBBR_0034; -.
DR   PATRIC; fig|518634.20.peg.36; -.
DR   KO; K01595; -.
DR   OrthoDB; POG091H040O; -.
DR   Proteomes; UP000003191; 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:UP000003191};
KW   Kinase {ECO:0000313|EMBL:EFE90177.1};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169, ECO:0000313|EMBL:EFE90177.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:EFE90177.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003191};
KW   Transferase {ECO:0000313|EMBL:EFE90177.1}.
FT   ACT_SITE    180    180       {ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    579    579       {ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   917 AA;  102563 MW;  83B8D1E280C576A2 CRC64;
     MATPEEQITP ADAAIVTTGT GRKGPEEHDL PQSLKDDMDL CLKILRDVLG EYNPELLSTF
     DTVRNYSVEA SAEHFAELED PNPAQDGLKE AVNVIDNMTL HDAQLLARAF ATYFHLANLS
     EENYRVSVLH ERENNVSGEQ AVDPINELTV AYHQLINEMG PAKAKELLDQ LEFHPVFTAH
     PTEARRKAVE GKIRRISELL GEYKILGGSD KKECLRRLYN EIDALFRTSP IALKKPTPVE
     EADTILDIFD NTLFHTIPKV YRRFDDWILG DQAGLVEPAC PAFFHPGSWI GSDRDGNPNV
     TAKVSRAVAR KFSDHVIAAL EEATRTVGRN LTMEAETTPP SAELKNLWSH QKEMSERLTD
     KAALISTKEM HRAVMLVMAD RLHYTIERDA DLMYHSCDDF LNDLKVVQRS LAEAGAKRSA
     YGPLQDLIWQ TETFGFHMVE MEFRQHSVVH ARALADIREH GLHGERGDLQ PMTHEVLDTF
     RALGAIQKRN GLKAARRYII SFTKSAQNIK DVYELNRLAF SHPEDVPTID VIPLFEQLED
     LQNSVDVLEE MIKIPEVQAR LKATGNKLEV MLGYSDSSKD AGPTSATLAL HSAQERIAKW
     AESHDIDLTL FHGRGGAVGR GGGPANRAVL AQPVGSVKCR FKLTEQGEVI FARYGNPVLA
     IRHVESVAAA TLLQSAPSVE KRNTDMTKKY ADMAAQLDEA AHNRFLDLLN TDGFAPWFSI
     VTPLTEIGLL PIGSRPAKRG LGAKSLDDLR TIPWIFSWAQ ARINLAAWYG LGTACEKFGD
     LETMRQAYEE WPLFSTFIDN IEMSIAKTDE RIAKMYLALG DREDLNKKVL EEMELTRKWV
     LDIVGDKWPL QHRHVLGQAI RIRSPYVDAL SVTQVLALKS LRKKVDKEEL SQSQQAGFIY
     LILCTVSGVA AGLQNTG
//
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