B-N-acetylhexosaminidase - Streptomyces plicatus

Preferred order of sections

Names and origin

Protein names

Submitted name:
B-N-acetylhexosaminidase EMBL AAC38798.3

Gene names

Name:

hex EMBL AAC38798.3

Organism

Streptomyces plicatus EMBL AAC38798.3

Taxonomic identifier

1922 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	506 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Technical term	3D-structure PDB 1M01 PDB 1M04 PDB 1JAK PDB 1HP4 PDB 1HP5 PDB 1M03
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

313 – 314

2

N-acetyl-D-glucosamine binding PDB 1M01 PDB 1M04 PDB 1M03

Region

393 – 395

3

N-acetyl-D-glucosamine binding PDB 1M01 PDB 1M04 PDB 1M03

Region

442 – 444

3

N-acetyl-D-glucosamine binding PDB 1M01 PDB 1M04 PDB 1M03

Sites

Binding site

162

1

N-acetyl-D-glucosamine PDB 1M01 PDB 1M04 PDB 1M03

Binding site

344

1

N-acetyl-D-glucosamine PDB 1M04 PDB 1M03

Binding site

361

1

N-acetyl-D-glucosamine PDB 1M01 PDB 1M04 PDB 1M03

Binding site

408

1

N-acetyl-D-glucosamine PDB 1M01 PDB 1M04 PDB 1M03

Sequences

Sequence

Length

Mass (Da)

Tools

O85361 [UniParc].

Last modified March 1, 2001. Version 3.
Checksum: E1A004A460C3610C
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FASTA

506

55,194

        10         20         30         40         50         60 
MTTGAAPDRK APVRPTPLDR VIPAPASVDP GGAPYRITRG THIRVDDSRE ARRVGDYLAD 

        70         80         90        100        110        120 
LLRPATGYRL PVTAHGHGGI RLRLAGGPYG DEGYRLDSGP AGVTITARKA AGLFHGVQTL 

       130        140        150        160        170        180 
RQLLPPAVEK DSAQPGPWLV AGGTIEDTPR YAWRSAMLDV SRHFFGVDEV KRYIDRVARY 

       190        200        210        220        230        240 
KYNKLHLHLS DDQGWRIAID SWPRLATYGG STEVGGGPGG YYTKAEYKEI VRYAASRHLE 

       250        260        270        280        290        300 
VVPEIDMPGH TNAALASYAE LNCDGVAPPL YTGTKVGFSS LCVDKDVTYD FVDDVIGELA 

       310        320        330        340        350        360 
ALTPGRYLHI GGDEAHSTPK ADFVAFMKRV QPIVAKYGKT VVGWHQLAGA EPVEGALVQY 

       370        380        390        400        410        420 
WGLDRTGDAE KAEVAEAARN GTGLILSPAD RTYLDMKYTK DTPLGLSWAG YVEVQRSYDW 

       430        440        450        460        470        480 
DPAGYLPGAP ADAVRGVEAP LWTETLSDPD QLDYMAFPRL PGVAELGWSP ASTHDWDTYK 

       490        500 
VRLAAQAPYW EAAGIDFYRS PQVPWT

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References

[1]	"Structural and functional characterization of Streptomyces plicatus beta-N-acetylhexosaminidase by comparative molecular modeling and site-directed mutagenesis." Mark B.L., Wasney G.A., Salo T.J., Khan A.R., Cao Z., Robbins P.W., James M.N., Triggs-Raine B.L. J. Biol. Chem. 273:19618-19624(1998) [PubMed: 9677388] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	Mark B.L. Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase." Mark B.L., Vocadlo D.J., Knapp S., Triggs-Raine B.L., Withers S.G., James M.N. J. Biol. Chem. 276:10330-10337(2001) [PubMed: 11124970] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 3-506.
[4]	"Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state." Williams S.J., Mark B.L., Vocadlo D.J., James M.N., Withers S.G. J. Biol. Chem. 277:40055-40065(2002) [PubMed: 12171933] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 3-506 IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.
[5]	"Biochemical and structural assessment of the 1-N-azasugar GalNAc-isofagomine as a potent family 20 beta-N-acetylhexosaminidase inhibitor." Mark B.L., Vocadlo D.J., Zhao D., Knapp S., Withers S.G., James M.N. J. Biol. Chem. 276:42131-42137(2001) [PubMed: 11522797] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-506.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF063001 Genomic DNA. Translation: AAC38798.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HP4	X-ray	2.20	A	3-506	[»]
1HP5	X-ray	2.10	A	3-506	[»]
1JAK	X-ray	1.75	A	3-506	[»]
1M01	X-ray	2.10	A	3-506	[»]
1M03	X-ray	1.90	A	3-506	[»]
1M04	X-ray	1.95	A	3-506	[»]

ProteinModelPortal

O85361.

SMR

O85361. Positions 8-506.

ModBase

Search...

Protein family/group databases

CAZy

GH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR001540. Glyco_hydro_20.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00728. Glyco_hydro_20. 1 hit.
[Graphical view]

PRINTS

PR00738. GLHYDRLASE20.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

O85361_STRPL

Accession

Primary (citable) accession number: O85361

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1998
Last sequence update:	March 1, 2001
Last modified:	July 27, 2011
This is version 46 of the entry and version 3 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)