Beta-galactosidase - Escherichia coli O157:H7

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Q8X685 (BGAL_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Beta-galactosidase
Short name=Beta-gal
EC=3.2.1.23

Alternative name(s):
Lactase

Gene names

Name:	lacZ
Ordered Locus Names:	Z0440, ECs0397

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	1024 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. HAMAP MF_01687
Cofactor	Binds 2 magnesium ions per monomer By similarity. HAMAP MF_01687 Binds 1 sodium ion per monomer By similarity. HAMAP MF_01687
Subunit structure	Homotetramer By similarity. HAMAP MF_01687
Sequence similarities	Belongs to the glycosyl hydrolase 2 family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding Sodium
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	beta-galactosidase complex Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1024

1024

Beta-galactosidase HAMAP MF_01687

PRO_0000366993

Regions

Region

538 – 541

Substrate binding By similarity

Sites

Active site

462

Proton donor By similarity

Active site

538

Nucleophile By similarity

Metal binding

202

Sodium By similarity

Metal binding

417

Magnesium 1 By similarity

Metal binding

419

Magnesium 1 By similarity

Metal binding

462

Magnesium 1 By similarity

Metal binding

598

Magnesium 2 By similarity

Metal binding

602

Sodium; via carbonyl oxygen By similarity

Metal binding

605

Sodium By similarity

Binding site

103

Substrate By similarity

Binding site

202

Substrate By similarity

Binding site

462

Substrate By similarity

Binding site

605

Substrate By similarity

Binding site

1000

Substrate By similarity

Site

358

Transition state stabilizer By similarity

Site

392

Transition state stabilizer By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8X685 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: B08BF1EBE7894FE3
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FASTA

1,024

116,410

        10         20         30         40         50         60 
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTNRPSQ QLRSLNGEWQ 

        70         80         90        100        110        120 
FVWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP 

       130        140        150        160        170        180 
TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLLS EFDLSAFLRA 

       190        200        210        220        230        240 
GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT LFNDDFSRAV 

       250        260        270        280        290        300 
LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLGLNVENPK 

       310        320        330        340        350        360 
LWSAEIPNIY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH 

       370        380        390        400        410        420 
HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG 

       430        440        450        460        470        480 
MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD 

       490        500        510        520        530        540 
PSRPVQYEGG GADTSATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA 

       550        560        570        580        590        600 
HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD LVDQSLIKYD ENGNPWSAYG GDFGDTPNDR 

       610        620        630        640        650        660 
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN ELLHWTVALD 

       670        680        690        700        710        720 
GKPLASGEVP LDVAPQGKQV IELPELPRLE STGQLWLTVH VVQPNATAWS EAGHISAWQQ 

       730        740        750        760        770        780 
WRLAENLSVT LPSAPHAIPQ LTTSETDFCI ELDNKRWQFN RQSGFLSQMW IGDKKQLLTP 

       790        800        810        820        830        840 
LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTV 

       850        860        870        880        890        900 
HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLTCQLA QVAERVNWLG 

       910        920        930        940        950        960 
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI 

       970        980        990       1000       1010       1020 
SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV 


WCQK

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References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG54693.1. BA000007 Genomic DNA. Translation: BAB33820.1.
PIR	A85529. E90678.
RefSeq	NP_286085.1. NC_002655.2. NP_308424.1. NC_002695.1.
3D structure databases
HSSP	HSSP built from PDB template 1PX3 based on UniProtKB P00722.
ProteinModelPortal	Q8X685.
SMR	Q8X685. Positions 14-1024.
ModBase	Search...
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000025339; EBESCP00000024232; EBESCG00000024393. EBESCT00000056636; EBESCP00000054464; EBESCG00000055684.
GeneID	914499. 957271.
GenomeReviews	Gene locus Z0440 in contig AE005174_GR. Gene locus ECs0397 in contig BA000007_GR.
KEGG	ece:Z0440. ecs:ECs0397.
PATRIC	18349741. VBIEscCol44059_0391.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000009399.
HOGENOM	HBG670643.
OMA	DFHVATH.
ProtClustDB	PRK09525.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS0397-MONOMER.
Family and domain databases
HAMAP	MF_01687. Beta_gal. [Tree]
InterPro	IPR004199. B-gal_small/dom_5. IPR008979. Galactose-bd-like. IPR011013. Glyco_hydro-type_carb-bd. IPR014718. Glyco_hydro-type_carb-bd_sub. IPR006101. Glyco_hydro_2. IPR013812. Glyco_hydro_2/20_Ig-like. IPR023232. Glyco_hydro_2_AS. IPR023933. Glyco_hydro_2_beta_Galsidase. IPR023230. Glyco_hydro_2_CS. IPR006102. Glyco_hydro_2_Ig-like. IPR006104. Glyco_hydro_2_N. IPR006103. Glyco_hydro_2_TIM. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 2 hits. G3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
KO	K01190.
Pfam	PF02929. Bgal_small_N. 1 hit. PF00703. Glyco_hydro_2. 1 hit. PF02836. Glyco_hydro_2_C. 1 hit. PF02837. Glyco_hydro_2_N. 1 hit. [Graphical view]
PRINTS	PR00132. GLHYDRLASE2.
SMART	SM01038. Bgal_small_N. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF74650. Gal_mut_like. 1 hit. SSF49303. Glyco_hydro_2Ig. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit. PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

BGAL_ECO57

Accession

Primary (citable) accession number: Q8X685
Secondary accession number(s): Q7AH58

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents