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Q54468

- CHB_SERMA

UniProt

Q54468 - CHB_SERMA

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Protein

Chitobiase

Gene
chb
Organism
Serratia marcescens
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Digests the beta-1,4-glycosidic bonds in N-acetylglucosamine (GlcNAc) oligomers (mainly dimers).

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei540 – 5401Proton donor

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

GO - Biological processi

  1. chitin catabolic process Source: UniProtKB-UniPathway
  2. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17688.
UniPathwayiUPA00349.

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitobiase (EC:3.2.1.52)
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene namesi
Name:chb
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

Subcellular locationi

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 885858ChitobiasePRO_0000012018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi56 ↔ 66
Disulfide bondi400 ↔ 408
Disulfide bondi505 ↔ 578

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
885
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 357
Beta strandi39 – 468
Helixi49 – 524
Turni56 – 605
Helixi62 – 643
Beta strandi66 – 7510
Beta strandi86 – 905
Beta strandi95 – 984
Beta strandi103 – 1075
Beta strandi112 – 1176
Beta strandi128 – 13811
Helixi143 – 1453
Beta strandi151 – 1533
Helixi163 – 1653
Beta strandi166 – 1683
Helixi170 – 1723
Turni179 – 1824
Helixi195 – 2017
Turni202 – 2043
Helixi210 – 2134
Beta strandi222 – 23211
Beta strandi237 – 2393
Helixi246 – 25813
Beta strandi267 – 2748
Helixi276 – 2783
Helixi281 – 2833
Beta strandi289 – 2935
Beta strandi298 – 3047
Helixi305 – 31814
Beta strandi321 – 3233
Beta strandi326 – 3349
Beta strandi339 – 3468
Beta strandi348 – 3503
Helixi354 – 36613
Beta strandi371 – 3755
Helixi391 – 3944
Turni395 – 3973
Beta strandi406 – 4094
Helixi426 – 43712
Turni438 – 4403
Beta strandi442 – 45211
Helixi454 – 46916
Helixi473 – 4786
Helixi498 – 5003
Helixi507 – 52620
Beta strandi534 – 5374
Helixi544 – 5463
Beta strandi550 – 5523
Beta strandi560 – 5634
Helixi565 – 5673
Turni571 – 5744
Helixi576 – 5838
Beta strandi586 – 5894
Helixi590 – 5923
Helixi593 – 60715
Beta strandi612 – 6165
Helixi617 – 6204
Beta strandi623 – 6253
Helixi626 – 6283
Beta strandi629 – 63810
Turni642 – 6454
Helixi646 – 65510
Beta strandi659 – 6624
Helixi665 – 6684
Beta strandi674 – 6763
Helixi692 – 6976
Beta strandi700 – 7023
Helixi703 – 7086
Beta strandi719 – 7213
Beta strandi730 – 7367
Helixi744 – 7518
Helixi754 – 76310
Beta strandi777 – 7793
Turni780 – 7823
Helixi788 – 80417
Helixi806 – 8127
Beta strandi823 – 8275
Beta strandi830 – 8345
Beta strandi840 – 8478
Helixi857 – 8593
Beta strandi868 – 8725

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7SX-ray1.80A28-885[»]
1C7TX-ray1.90A28-885[»]
1QBAX-ray1.85A28-885[»]
1QBBX-ray2.00A28-885[»]
ProteinModelPortaliQ54468.
SMRiQ54468. Positions 28-885.

Miscellaneous databases

EvolutionaryTraceiQ54468.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProiIPR025705. Beta_hexosaminidase_sua/sub.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR004866. CHB/HEX_N_dom.
IPR004867. CHB_HEX_C_dom.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF03173. CHB_HEX. 1 hit.
PF03174. CHB_HEX_C. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSiPR00738. GLHYDRLASE20.
SMARTiSM01081. CHB_HEX. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q54468-1 [UniParc]FASTAAdd to Basket

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MNAFKLSALA RLTATMGFLG GMGSAMADQQ LVDQLSQLKL NVKMLDNRAG    50
ENGVDCAALG ADWASCNRVL FTLSNDGQAI DGKDWVIYFH SPRQTLRVDN 100
DQFKIAHLTG DLYKLEPTAK FSGFPAGKAV EIPVVAEYWQ LFRNDFLPRW 150
YATSGDAKPK MLANTDTENL DQFVAPFTGD QWKRTKDDKN ILMTPASRFV 200
SNADLQTLPA GALRGKIVPT PMQVKVHAQD ADLRKGVALD LSTLVKPAAD 250
VVSQRFALLG VPVQTNGYPI KTDIQPGKFK GAMAVSGAYE LKIGKKEAQV 300
IGFDQAGVFY GLQSILSLVP SDGSGKIATL DASDAPRFPY RGIFLDVARN 350
FHKKDAVLRL LDQMAAYKLN KFHFHLSDDE GWRIEIPGLP ELTEVGGQRC 400
HDLSETTCLL PQYGQGPDVY GGFFSRQDYI DIIKYAQARQ IEVIPEIDMP 450
AHARAAVVSM EARYKKLHAA GKEQEANEFR LVDPTDTSNT TSVQFFNRQS 500
YLNPCLDSSQ RFVDKVIGEI AQMHKEAGQP IKTWHFGGDE AKNIRLGAGY 550
TDKAKPEPGK GIIDQSNEDK PWAKSQVCQT MIKEGKVADM EHLPSYFGQE 600
VSKLVKAHGI DRMQAWQDGL KDAESSKAFA TSRVGVNFWD TLYWGGFDSV 650
NDWANKGYEV VVSNPDYVYM DFPYEVNPDE RGYYWGTRFS DERKVFSFAP 700
DNMPQNAETS VDRDGNHFNA KSDKPWPGAY GLSAQLWSET QRTDPQMEYM 750
IFPRALSVAE RSWHRAGWEQ DYRAGREYKG GETHFVDTQA LEKDWLRFAN 800
ILGQRELAKL DKGGVAYRLP VPGARVAAGK LEANIALPGL GIEYSTDGGK 850
QWQRYDAKAK PAVSGEVQVR SVSPDGKRYS RAEKV 885
Length:885
Mass (Da):98,548
Last modified:November 1, 1996 - v1
Checksum:iA749CC0F507DE2E1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L43594 Genomic DNA. Translation: AAB03808.1.
PIRiJC4732.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L43594 Genomic DNA. Translation: AAB03808.1 .
PIRi JC4732.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C7S X-ray 1.80 A 28-885 [» ]
1C7T X-ray 1.90 A 28-885 [» ]
1QBA X-ray 1.85 A 28-885 [» ]
1QBB X-ray 2.00 A 28-885 [» ]
ProteinModelPortali Q54468.
SMRi Q54468. Positions 28-885.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00349 .
BioCyci MetaCyc:MONOMER-17688.

Miscellaneous databases

EvolutionaryTracei Q54468.

Family and domain databases

Gene3Di 2.60.40.290. 1 hit.
2.60.40.320. 1 hit.
3.20.20.80. 1 hit.
3.30.379.10. 1 hit.
InterProi IPR025705. Beta_hexosaminidase_sua/sub.
IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR004866. CHB/HEX_N_dom.
IPR004867. CHB_HEX_C_dom.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
IPR014756. Ig_E-set.
[Graphical view ]
Pfami PF03173. CHB_HEX. 1 hit.
PF03174. CHB_HEX_C. 1 hit.
PF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view ]
PRINTSi PR00738. GLHYDRLASE20.
SMARTi SM01081. CHB_HEX. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF55545. SSF55545. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "N-acetylglucosaminidase (chitobiase) from Serratia marcescens: gene sequence, and protein production and purification in Escherichia coli."
    Tews I., Vincentelli R., Vorgias C.E.
    Gene 170:63-67(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease."
    Tews I., Perrakis A., Oppenheim A., Dauter Z., Wilson K.S., Vorgias C.E.
    Nat. Struct. Biol. 3:638-648(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).

Entry informationi

Entry nameiCHB_SERMA
AccessioniPrimary (citable) accession number: Q54468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 100 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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