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Database: UniProt/TrEMBL
Entry: A0A0A0U8I9_BIFLN
LinkDB: A0A0A0U8I9_BIFLN
Original site: A0A0A0U8I9_BIFLN 
ID   A0A0A0U8I9_BIFLN        Unreviewed;       917 AA.
AC   A0A0A0U8I9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   07-JUN-2017, entry version 19.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|SAAS:SAAS00635171};
DE            EC=4.1.1.31 {ECO:0000256|SAAS:SAAS00635171};
GN   ORFNames=BLGT_00475 {ECO:0000313|EMBL:AIW43115.1};
OS   Bifidobacterium longum subsp. longum GT15.
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=1300227 {ECO:0000313|EMBL:AIW43115.1, ECO:0000313|Proteomes:UP000030089};
RN   [1] {ECO:0000313|EMBL:AIW43115.1, ECO:0000313|Proteomes:UP000030089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GT15 {ECO:0000313|EMBL:AIW43115.1,
RC   ECO:0000313|Proteomes:UP000030089};
RA   Danilenko V.N., Zakharevich N.V., Averina O.V.;
RT   "Complete genome sequence of Bifidobacterium longum subsp. longum
RT   GT15.";
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.
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; CP006741; AIW43115.1; -; Genomic_DNA.
DR   RefSeq; WP_038426231.1; NZ_CP006741.1.
DR   EnsemblBacteria; AIW43115; AIW43115; BLGT_00475.
DR   KEGG; blz:BLGT_00475; -.
DR   KO; K01595; -.
DR   Proteomes; UP000030089; 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:UP000030089};
KW   Lyase {ECO:0000256|SAAS:SAAS00635169};
KW   Magnesium {ECO:0000256|SAAS:SAAS00635157};
KW   Pyruvate {ECO:0000313|EMBL:AIW43115.1}.
FT   ACT_SITE    180    180       {ECO:0000256|PROSITE-ProRule:PRU10111}.
FT   ACT_SITE    579    579       {ECO:0000256|PROSITE-ProRule:PRU10112}.
SQ   SEQUENCE   917 AA;  102657 MW;  8176ED1CA17C96C6 CRC64;
     MATPEEQITP ADAAIVTTGT GRKGPEEHDL PESLKYDMDL CLEILRNVLG EYNPELLSTF
     DTVRHYAVEA SAEHFAELKD PNPDQDGLKE AVNVIDNMTL HDAQLLARAF ATYFHLANLS
     EENYRVSVLH ERENNVPVDQ AVDPINELTV AYHQLINETG PAKAKELLNQ LEFHPVFTAH
     PTEARRKAVE GKIRRVSELL EEYKRLGGSD KKECLRRLYN EIDALFRTSP IALKKPTPVE
     EADTILDIFD NTLFNTIPKV YRRFDDWVLG DKAGLVEPAC PAFFHPGSWI GSDRDGNPNV
     TAKVSRAVAR KFSDHVIAAL EQATRTVGRN LTMEAETTPP SAELKNLWSH QKEMSERLTD
     KAALISTKEM HRAVMLVMAD RLHYTIERDA DLMYHSCDNF LADLKVVQRS LAAAGAKRSA
     YGPLQDLIWQ TETFGFHMVE MEFRQHSVVH ARALADIREH GLHGERGELQ PMTHEVLDTF
     RALGAIQKRN GLKAARRYII SFTKSAQNIK DVYELNRLAF SHPEDVPTID VIPLFEQLED
     LQNSVDVLEE MIKIPEVQAR LKATGNKLEV MLGYSDSSKD AGPTSATLAL HSAQERIAKW
     AESHDIDLTL FHGRGGAVGR GGGPANRAVL AQPVGSVKCR FKLTEQGEVI FARYGNPVLA
     IRHVESVAAA TLLQSAPSVE KRNTEMTEKY ADMAAQLDEA AHNRFLDLLN TDGFAPWFSI
     VTPLTEIGLL PIGSRPAKRG LGAKSLDDLR TIPWIFSWAQ ARINLAAWYG LGTACEKFGD
     LETMRQAYEE WPLFSTFIDN IEMSIAKTDE RIARMYLALG DREDLNEKVL NEMELTRKWV
     LAIVGDKWPL QHRHVLGQAI RIRSPYVDAL SVTQVLALRS LRKKVDKEEL SQSQQAGFIY
     LILCTVSGVA AGLQNTG
//
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