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Protein

Exo-beta-D-glucosaminidase

Gene

csxA

Organism
Amycolatopsis orientalis (Nocardia orientalis)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide.2 Publications

Catalytic activityi

Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.2 Publications

pH dependencei

Optimum pH is 5.5 with chitotriitol as substrate, and 5.3 with (GlcN)2 as substrate. Activity is lost below pH 3.5 and above pH 8.0.2 Publications

Temperature dependencei

Optimum temperature is 60 degrees Celsius. Stable below 50 degrees Celsius, inactive above 60 degrees Celsius.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei469Proton donor1 Publication1
Active sitei541Nucleophile1 Publication1

GO - Molecular functioni

GO - Biological processi

  • chitin catabolic process Source: UniProtKB-KW
  • polysaccharide catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.165. 315.

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Exo-beta-D-glucosaminidaseImported (EC:3.2.1.165)
Short name:
GlcNase1 Publication
Alternative name(s):
Exochitinase1 Publication
Gene namesi
Name:csxAImported
OrganismiAmycolatopsis orientalis (Nocardia orientalis)
Taxonomic identifieri31958 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaPseudonocardialesPseudonocardiaceaeAmycolatopsis

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
PropeptideiPRO_000039904633 – 46Sequence analysis1 PublicationAdd BLAST14
ChainiPRO_500009579947 – 1032Exo-beta-D-glucosaminidase1 PublicationAdd BLAST986

Interactioni

Subunit structurei

Monomer.3 Publications

Structurei

Secondary structure

11032
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi51 – 53Combined sources3
Beta strandi56 – 61Combined sources6
Helixi62 – 64Combined sources3
Helixi68 – 70Combined sources3
Beta strandi82 – 85Combined sources4
Helixi90 – 96Combined sources7
Helixi108 – 111Combined sources4
Helixi115 – 117Combined sources3
Beta strandi121 – 130Combined sources10
Beta strandi133 – 140Combined sources8
Beta strandi143 – 151Combined sources9
Beta strandi154 – 157Combined sources4
Turni159 – 161Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi169 – 172Combined sources4
Turni174 – 176Combined sources3
Beta strandi179 – 188Combined sources10
Turni193 – 195Combined sources3
Beta strandi196 – 198Combined sources3
Turni202 – 204Combined sources3
Turni209 – 212Combined sources4
Beta strandi219 – 238Combined sources20
Beta strandi242 – 255Combined sources14
Beta strandi257 – 259Combined sources3
Beta strandi261 – 269Combined sources9
Beta strandi272 – 280Combined sources9
Beta strandi285 – 289Combined sources5
Beta strandi293 – 297Combined sources5
Turni304 – 306Combined sources3
Beta strandi312 – 320Combined sources9
Beta strandi323 – 332Combined sources10
Beta strandi337 – 341Combined sources5
Beta strandi347 – 351Combined sources5
Beta strandi354 – 356Combined sources3
Beta strandi358 – 362Combined sources5
Helixi373 – 385Combined sources13
Beta strandi390 – 395Combined sources6
Helixi400 – 409Combined sources10
Beta strandi412 – 416Combined sources5
Beta strandi419 – 421Combined sources3
Helixi422 – 424Combined sources3
Turni425 – 427Combined sources3
Beta strandi431 – 433Combined sources3
Helixi440 – 455Combined sources16
Beta strandi464 – 466Combined sources3
Beta strandi468 – 470Combined sources3
Helixi474 – 486Combined sources13
Beta strandi493 – 495Combined sources3
Beta strandi497 – 499Combined sources3
Beta strandi503 – 505Combined sources3
Helixi521 – 525Combined sources5
Beta strandi534 – 542Combined sources9
Helixi551 – 557Combined sources7
Helixi560 – 568Combined sources9
Turni575 – 577Combined sources3
Beta strandi579 – 581Combined sources3
Helixi587 – 597Combined sources11
Helixi603 – 628Combined sources26
Beta strandi632 – 634Combined sources3
Beta strandi636 – 642Combined sources7
Beta strandi647 – 649Combined sources3
Beta strandi651 – 653Combined sources3
Helixi664 – 672Combined sources9
Beta strandi675 – 680Combined sources6
Turni682 – 684Combined sources3
Beta strandi686 – 691Combined sources6
Beta strandi693 – 695Combined sources3
Beta strandi697 – 708Combined sources12
Beta strandi713 – 724Combined sources12
Turni726 – 728Combined sources3
Beta strandi729 – 735Combined sources7
Beta strandi744 – 753Combined sources10
Beta strandi759 – 770Combined sources12
Helixi776 – 778Combined sources3
Beta strandi786 – 788Combined sources3
Helixi793 – 797Combined sources5
Beta strandi803 – 811Combined sources9
Beta strandi815 – 825Combined sources11
Beta strandi828 – 830Combined sources3
Beta strandi833 – 841Combined sources9
Beta strandi852 – 855Combined sources4
Beta strandi857 – 860Combined sources4
Beta strandi865 – 873Combined sources9
Helixi874 – 877Combined sources4
Beta strandi883 – 888Combined sources6
Turni889 – 891Combined sources3
Beta strandi892 – 897Combined sources6
Beta strandi909 – 912Combined sources4
Helixi913 – 915Combined sources3
Beta strandi916 – 924Combined sources9
Beta strandi935 – 938Combined sources4
Beta strandi945 – 965Combined sources21
Beta strandi968 – 970Combined sources3
Beta strandi974 – 978Combined sources5
Beta strandi981 – 987Combined sources7
Beta strandi999 – 1007Combined sources9
Beta strandi1009 – 1018Combined sources10
Beta strandi1026 – 1032Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VZOX-ray2.24A/B2-1032[»]
2VZPX-ray1.05A/B906-1032[»]
2VZQX-ray1.70A/B906-1032[»]
2VZRX-ray1.95A/B906-1032[»]
2VZSX-ray1.85A/B2-1032[»]
2VZTX-ray2.20A/B2-1032[»]
2VZUX-ray2.10A/B2-1032[»]
2VZVX-ray2.70A/B2-1032[»]
2X05X-ray2.30A/B2-1032[»]
2X09X-ray2.40A/B2-1032[»]
ProteinModelPortaliQ56F26.
SMRiQ56F26.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56F26.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini909 – 1032CBM6PROSITE-ProRule annotationAdd BLAST124

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.Sequence analysis
Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

KOiK15855.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR005084. CMB_fam6.
IPR028829. Exo-b-D-glucosamin.
IPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10066:SF66. PTHR10066:SF66. 1 hit.
PfamiPF16990. CBM_35. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q56F26-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRQKRTRI PLLAMTVTAL AAAVCGVTTA PAATGAEVAV PLSVGAAAGN
60 70 80 90 100
ATPIPGYVIQ SSAQVSDDSA VSKPGFPTSG WYPVSSRSTV YAGLLQNGKY
110 120 130 140 150
ADPFYSTNMQ NVPAAQFSVP WWYRTDLNVD DTSSRTYLDF SGVLSKADVW
160 170 180 190 200
VNGTKVATKD QVNGAYTRHD LDITAQVHTG VNSVAFKVYP NDPNRDLSMG
210 220 230 240 250
WIDWAQTPPD QNMGIVRDVL VRRSGAVALR SAHVIQKLNS ALDHADLTVK
260 270 280 290 300
ADVRNDSANA VQTTVAGTVA GKPISQTVSL AAKERKTVTF PLVGLDRPNV
310 320 330 340 350
WWPAGMGGQH RYDLDLTASV GGTPSDAAKS KFGVRDVKAT LNSSGGRQYS
360 370 380 390 400
VNGKPLLIRG GGYTPDLFLR WNETAAADKL KYVLNLGLNT VRLEGHIEPD
410 420 430 440 450
EFFDIADDLG VLTMPGWECC DKWEGQVNGE EKGEPWVESD YPIAKASMFS
460 470 480 490 500
EAERLRDHPS VISFHIGSDF APDRRIEQGY LDAMKAADFL LPVIPAASAR
510 520 530 540 550
PSPITGASGM KMNGPYDYVP PVYWYDKSQK DRGGAWSFNS ETSAGVDIPT
560 570 580 590 600
MDTLKRMMSA SELDTMWKNP SAKQYHRSSS DTFGNLKLFG DALTKRYGAS
610 620 630 640 650
ANLNDFVRKA QLSQYENVRA EFESHSRNYT DSTNPSTGLI YWMLNSPWTS
660 670 680 690 700
LHWQLFDAYM DQNGAYYGAK KANEPLHIQY SHDNRSVVVI NQTSNAVSGL
710 720 730 740 750
TATTKLYNLD GTEKYSNTKT GLSVGALGAK ATAVTVPAVS GLSTTYLAKW
760 770 780 790 800
VLTDSSGKEV SRNVYWLSTK ADTLNWGGSD WYYTPQSAFA DLSGLNNLGQ
810 820 830 840 850
SAVGATANSV AGADGTTTTT VTLKNTSGGR LPAFYVDSKV VDSAGKPVLP
860 870 880 890 900
VEWNDNAVSL WPGETTTLTA KYRTADLKGS KPSVRISGWN TGTQTVPADG
910 920 930 940 950
SGPGPSDPVD YQAEDATIVQ GAVESNHAGY TGTGFVNYDN VAGSSVEWTV
960 970 980 990 1000
TVPSAGTYDV VVRYANGTTT SRPLDFSVNG SISASGVAFG STGTWPAWTT
1010 1020 1030
KTVRVTLAAG VNKIKAVATT ANGGPNVDKI TL
Length:1,032
Mass (Da):110,633
Last modified:March 21, 2006 - v2
Checksum:i150778589094F223
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti58V → VN AA sequence (PubMed:16316314).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY962188 Genomic DNA. Translation: AAX62629.2.

Genome annotation databases

KEGGiag:AAX62629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY962188 Genomic DNA. Translation: AAX62629.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VZOX-ray2.24A/B2-1032[»]
2VZPX-ray1.05A/B906-1032[»]
2VZQX-ray1.70A/B906-1032[»]
2VZRX-ray1.95A/B906-1032[»]
2VZSX-ray1.85A/B2-1032[»]
2VZTX-ray2.20A/B2-1032[»]
2VZUX-ray2.10A/B2-1032[»]
2VZVX-ray2.70A/B2-1032[»]
2X05X-ray2.30A/B2-1032[»]
2X09X-ray2.40A/B2-1032[»]
ProteinModelPortaliQ56F26.
SMRiQ56F26.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM35. Carbohydrate-Binding Module Family 35.
GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAX62629.

Phylogenomic databases

KOiK15855.

Enzyme and pathway databases

BRENDAi3.2.1.165. 315.

Miscellaneous databases

EvolutionaryTraceiQ56F26.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.320. 1 hit.
3.20.20.80. 2 hits.
InterProiIPR005084. CMB_fam6.
IPR028829. Exo-b-D-glucosamin.
IPR008979. Galactose-bd-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR10066:SF66. PTHR10066:SF66. 1 hit.
PfamiPF16990. CBM_35. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 3 hits.
SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51175. CBM6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEBDG_AMYOR
AccessioniPrimary (citable) accession number: Q56F26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 21, 2006
Last modified: November 2, 2016
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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.