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Protein
Submitted name:

6-phospho-beta-glucosidase A

Gene

ECO111_1930

Organism
Escherichia coli O111:H- (strain 11128 / EHEC)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Enzyme and pathway databases

BioCyciECOL585396:GJCW-1985-MONOMER.

Names & Taxonomyi

Protein namesi
Submitted name:
6-phospho-beta-glucosidase AImported
Gene namesi
Ordered Locus Names:ECO111_1930Imported
OrganismiEscherichia coli O111:H- (strain 11128 / EHEC)Imported
Taxonomic identifieri585396 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001614 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliC8UPX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 1 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
KOiK01223.
OMAiEDREPVM.
OrthoDBiEOG6F81PM.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C8UPX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGFKKGFLW GGAVAAHQLE GGWNEGGKGI SIADVMTAGA HGVPREVTEG
60 70 80 90 100
VIDGLNYPNH EAIDFYHRYK TDIQLFAEMG FKCFRTSIVW TRIFPQGDEQ
110 120 130 140 150
EPNEEGLQFY DDLFDECLKQ GMEPVVTLSH FEMPYHLVTK YGGWRNRKLI
160 170 180 190 200
DFFIRFASTV FTRYKEKVKY WMTFNEINNQ VNFSESLCPF TNSGILYSPE
210 220 230 240 250
EDINEREQIM YQAVHYELVA SALAVQTGKS INPEFNIGCM IAMCPIYPLT
260 270 280 290 300
CAPNDMMMAT KAMHRRYWFT DVHARGYYPQ HMLNYFARKG FNLDITPEDN
310 320 330 340 350
AILASGCVDF IGFSYYMSFT TQFSPDNPQL DYVEPRDLVS NPYIDTSEWG
360 370 380 390 400
WQIDPAGLRY SLNWFWDHFQ LPLFIVENGF GAVDQRQADG TVNDHYRIDY
410 420 430 440 450
FASHIREMKK AVVEDGVDLI GYTPWGCIDL VSAGTGEMKK RYGMIYVDKD
460 470
NEGKGTLERI RKASFYWYRD LIANNGENI
Length:479
Mass (Da):55,215
Last modified:November 3, 2009 - v1
Checksum:iD963C165FD0509A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010960 Genomic DNA. Translation: BAI35822.1.
RefSeqiWP_000012625.1. NC_013364.1.

Genome annotation databases

EnsemblBacteriaiBAI35822; BAI35822; ECO111_1930.
KEGGieoi:ECO111_1930.
PATRICi32107101. VBIEscCol143187_2009.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010960 Genomic DNA. Translation: BAI35822.1.
RefSeqiWP_000012625.1. NC_013364.1.

3D structure databases

ProteinModelPortaliC8UPX2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAI35822; BAI35822; ECO111_1930.
KEGGieoi:ECO111_1930.
PATRICi32107101. VBIEscCol143187_2009.

Phylogenomic databases

eggNOGiCOG2723.
HOGENOMiHOG000088631.
KOiK01223.
OMAiEDREPVM.
OrthoDBiEOG6F81PM.

Enzyme and pathway databases

BioCyciECOL585396:GJCW-1985-MONOMER.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001360. Glyco_hydro_1.
IPR018120. Glyco_hydro_1_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10353. PTHR10353. 1 hit.
PfamiPF00232. Glyco_hydro_1. 1 hit.
[Graphical view]
PRINTSiPR00131. GLHYDRLASE1.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00572. GLYCOSYL_HYDROL_F1_1. 1 hit.
PS00653. GLYCOSYL_HYDROL_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
    Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
    Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 11128 / EHECImported.

Entry informationi

Entry nameiC8UPX2_ECO1A
AccessioniPrimary (citable) accession number: C8UPX2
Entry historyi
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: July 22, 2015
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.