(data stored in ACNUC8465 zone)

HOGENOM: ESCOL1_1_PE2658

ID   ESCOL1_1_PE2658                      STANDARD;      PRT;   188 AA.
AC   ESCOL1_1_PE2658; P77475;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Phosphatase YqaB; EC=3.1.3 -; (ESCOL1_1.PE2658).
GN   Name=yqaB; OrderedLocusNames=b2690, JW2665;
OS   ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=511145;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ESCOL1_1.PE2658.
CC       Escherichia coli str. K-12 substr. MG1655 chromosome, complete genome.
CC       pEp5, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:YQAB_ECOLI
CC   -!- FUNCTION: Catalyzes the dephosphorylation of the artificial
CC       chromogenic substrate p-nitrophenyl phosphate (pNPP) and of the
CC       natural substrates fructose 1-phosphate and 6-phosphogluconate.
CC   -!- INTERACTION:
CC       P50456:mlc; NbExp=1; IntAct=EBI-371245, EBI-1116104;
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family.
CC   -!- GENE_FAMILY: HOG000248341 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P77475; -.
DR   EMBL; U00096; AAC75737.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16557.1; -; Genomic_DNA.
DR   PIR; C65049; C65049.
DR   RefSeq; AP_003262.1; AC_000091.1.
DR   RefSeq; NP_417175.1; NC_000913.2.
DR   ProteinModelPortal; P77475; -.
DR   SMR; P77475; 3-187.
DR   DIP; DIP-12842N; -.
DR   IntAct; P77475; 5.
DR   MINT; MINT-1265616; -.
DR   EnsemblBacteria; EBESCT00000001473; EBESCP00000001473; EBESCG00000001224.
DR   EnsemblBacteria; EBESCT00000015289; EBESCP00000014580; EBESCG00000014349.
DR   GeneID; 945776; -.
DR   GenomeReviews; AP009048_GR; JW2665.
DR   GenomeReviews; U00096_GR; b2690.
DR   KEGG; ecj:JW2665; -.
DR   KEGG; eco:b2690; -.
DR   EchoBASE; EB3301; -.
DR   EcoGene; EG13530; yqaB.
DR   eggNOG; COG0637; -.
DR   GeneTree; EBGT00050000009691; -.
DR   OMA; HRKAWDE; -.
DR   ProtClustDB; PRK10725; -.
DR   BioCyc; EcoCyc:G7408-MON; -.
DR   BioCyc; MetaCyc:G7408-MON; -.
DR   Genevestigator; P77475; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR010976; B-phosphoglucomutase_hydrolase.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006402; HAD-SF_hydro_IA_v3.
DR   InterPro; IPR005833; Haloacid_DH/epoxide_hydro.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
DR   TIGRFAMs; TIGR02009; PGMB-YQAB-SF; 1.
DR   HOGENOMDNA; ESCOL1_1.PE2658; -.
KW   Complete proteome; Hydrolase; Reference proteome.
SQ   SEQUENCE   188 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MYERYAGLIF DMDGTILDTE PTHRKAWREV LGHYGLQYDI QAMIALNGSP TWRIAQAIIE
     LNQADLDPHA LAREKTEAVR SMLLDSVEPL PLVDVVKSWH GRRPMAVGTG SESAIAEALL
     AHLGLRHYFD AVVAADHVKH HKPAPDTFLL CAQRMGVQPT QCVVFEDADF GIQAARAAGM
     DAVDVRLL
//

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