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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)DescriptionActionsGraphical viewLength
Binding sitei162N-acetyl-D-glucosamineCombined sources1
Binding sitei344N-acetyl-D-glucosamineCombined sources1
Binding sitei361N-acetyl-D-glucosamineCombined sources1
Binding sitei408N-acetyl-D-glucosamineCombined sources1

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 databases

ChEMBLiCHEMBL1075027.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi263 ↔ 282Combined sources

Interactioni

Chemistry databases

BindingDBiO85361.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO85361.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 147Glyco_hydro_20bInterPro annotationAdd BLAST128
Domaini151 – 317Glyco_hydro_20InterPro annotationAdd BLAST167
Domaini325 – 470Glyco_hydro_20InterPro annotationAdd BLAST146

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni313 – 314N-acetyl-D-glucosamine bindingCombined sources2
Regioni393 – 395N-acetyl-D-glucosamine bindingCombined sources3
Regioni442 – 444N-acetyl-D-glucosamine bindingCombined sources3

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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...

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: November 2, 2016
This is version 78 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.