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Protein
Submitted name:

B-N-acetylhexosaminidase

Gene

hex

Organism
Streptomyces plicatus
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei162 – 1621N-acetyl-D-glucosamineCombined sources
Binding sitei344 – 3441N-acetyl-D-glucosamineCombined sources
Binding sitei361 – 3611N-acetyl-D-glucosamineCombined sources
Binding sitei408 – 4081N-acetyl-D-glucosamineCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BRENDAi3.2.1.52. 6076.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
Submitted name:
B-N-acetylhexosaminidaseImported
Gene namesi
Name:hexImported
OrganismiStreptomyces plicatusImported
Taxonomic identifieri1922 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1075027.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi263 ↔ 282Combined sources

Interactioni

Chemistry

BindingDBiO85361.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HP4X-ray2.20A3-506[»]
1HP5X-ray2.10A3-506[»]
1JAKX-ray1.75A3-506[»]
1M01X-ray2.10A3-506[»]
1M03X-ray1.90A3-506[»]
1M04X-ray1.95A3-506[»]
ProteinModelPortaliO85361.
SMRiO85361. Positions 8-506.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO85361.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 147128Glyco_hydro_20bInterPro annotationAdd
BLAST
Domaini151 – 317167Glyco_hydro_20InterPro annotationAdd
BLAST
Domaini325 – 470146Glyco_hydro_20InterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni313 – 3142N-acetyl-D-glucosamine bindingCombined sources
Regioni393 – 3953N-acetyl-D-glucosamine bindingCombined sources
Regioni442 – 4443N-acetyl-D-glucosamine bindingCombined sources

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
[Graphical view]
PfamiPF00728. Glyco_hydro_20. 2 hits.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.

Sequencei

Sequence statusi: Complete.

O85361-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTGAAPDRK APVRPTPLDR VIPAPASVDP GGAPYRITRG THIRVDDSRE
60 70 80 90 100
ARRVGDYLAD LLRPATGYRL PVTAHGHGGI RLRLAGGPYG DEGYRLDSGP
110 120 130 140 150
AGVTITARKA AGLFHGVQTL RQLLPPAVEK DSAQPGPWLV AGGTIEDTPR
160 170 180 190 200
YAWRSAMLDV SRHFFGVDEV KRYIDRVARY KYNKLHLHLS DDQGWRIAID
210 220 230 240 250
SWPRLATYGG STEVGGGPGG YYTKAEYKEI VRYAASRHLE VVPEIDMPGH
260 270 280 290 300
TNAALASYAE LNCDGVAPPL YTGTKVGFSS LCVDKDVTYD FVDDVIGELA
310 320 330 340 350
ALTPGRYLHI GGDEAHSTPK ADFVAFMKRV QPIVAKYGKT VVGWHQLAGA
360 370 380 390 400
EPVEGALVQY WGLDRTGDAE KAEVAEAARN GTGLILSPAD RTYLDMKYTK
410 420 430 440 450
DTPLGLSWAG YVEVQRSYDW DPAGYLPGAP ADAVRGVEAP LWTETLSDPD
460 470 480 490 500
QLDYMAFPRL PGVAELGWSP ASTHDWDTYK VRLAAQAPYW EAAGIDFYRS

PQVPWT
Length:506
Mass (Da):55,194
Last modified:March 1, 2001 - v3
Checksum:iE1A004A460C3610C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063001 Genomic DNA. Translation: AAC38798.3.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF063001 Genomic DNA. Translation: AAC38798.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HP4X-ray2.20A3-506[»]
1HP5X-ray2.10A3-506[»]
1JAKX-ray1.75A3-506[»]
1M01X-ray2.10A3-506[»]
1M03X-ray1.90A3-506[»]
1M04X-ray1.95A3-506[»]
ProteinModelPortaliO85361.
SMRiO85361. Positions 8-506.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiO85361.
ChEMBLiCHEMBL1075027.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.52. 6076.

Miscellaneous databases

EvolutionaryTraceiO85361.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR015883. Glyco_hydro_20_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
[Graphical view]
PfamiPF00728. Glyco_hydro_20. 2 hits.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSiPR00738. GLHYDRLASE20.
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.S., Khan A.R., Cao Z., Robbins P.W., James M.N.G., Triggs-Raine B.L.
    J. Biol. Chem. 273:19618-19624(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Eder C.M., Forkmann G.
    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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 3-506, DISULFIDE BONDS.
  4. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3-506, DISULFIDE BONDS.
  5. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 3-506 IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE, DISULFIDE BONDS.

Entry informationi

Entry nameiO85361_STRPL
AccessioniPrimary (citable) accession number: O85361
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: March 1, 2001
Last modified: April 13, 2016
This is version 76 of the entry and version 3 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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 one 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.