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Protein

Chitobiase

Gene

chb

Organism
Serratia marcescens
Status
Reviewed-Annotation score: Annotation score: 4 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: chitin degradation

This protein is involved in the pathway chitin degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway chitin degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei540Proton donor1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeSerratia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000001201828 – 885ChitobiaseAdd BLAST858

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi56 ↔ 66
Disulfide bondi400 ↔ 408
Disulfide bondi505 ↔ 578

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1885
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 35Combined sources7
Beta strandi39 – 46Combined sources8
Helixi49 – 52Combined sources4
Turni56 – 60Combined sources5
Helixi62 – 64Combined sources3
Beta strandi66 – 75Combined sources10
Beta strandi86 – 90Combined sources5
Beta strandi95 – 98Combined sources4
Beta strandi103 – 107Combined sources5
Beta strandi112 – 117Combined sources6
Beta strandi128 – 138Combined sources11
Helixi143 – 145Combined sources3
Beta strandi151 – 153Combined sources3
Helixi163 – 165Combined sources3
Beta strandi166 – 168Combined sources3
Helixi170 – 172Combined sources3
Turni179 – 182Combined sources4
Helixi195 – 201Combined sources7
Turni202 – 204Combined sources3
Helixi210 – 213Combined sources4
Beta strandi222 – 232Combined sources11
Beta strandi237 – 239Combined sources3
Helixi246 – 258Combined sources13
Beta strandi267 – 274Combined sources8
Helixi276 – 278Combined sources3
Helixi281 – 283Combined sources3
Beta strandi289 – 293Combined sources5
Beta strandi298 – 304Combined sources7
Helixi305 – 318Combined sources14
Beta strandi321 – 323Combined sources3
Beta strandi326 – 334Combined sources9
Beta strandi339 – 346Combined sources8
Beta strandi348 – 350Combined sources3
Helixi354 – 366Combined sources13
Beta strandi371 – 375Combined sources5
Helixi391 – 394Combined sources4
Turni395 – 397Combined sources3
Beta strandi406 – 409Combined sources4
Helixi426 – 437Combined sources12
Turni438 – 440Combined sources3
Beta strandi442 – 452Combined sources11
Helixi454 – 469Combined sources16
Helixi473 – 478Combined sources6
Helixi498 – 500Combined sources3
Helixi507 – 526Combined sources20
Beta strandi534 – 537Combined sources4
Helixi544 – 546Combined sources3
Beta strandi550 – 552Combined sources3
Beta strandi560 – 563Combined sources4
Helixi565 – 567Combined sources3
Turni571 – 574Combined sources4
Helixi576 – 583Combined sources8
Beta strandi586 – 589Combined sources4
Helixi590 – 592Combined sources3
Helixi593 – 607Combined sources15
Beta strandi612 – 616Combined sources5
Helixi617 – 620Combined sources4
Beta strandi623 – 625Combined sources3
Helixi626 – 628Combined sources3
Beta strandi629 – 638Combined sources10
Turni642 – 645Combined sources4
Helixi646 – 655Combined sources10
Beta strandi659 – 662Combined sources4
Helixi665 – 668Combined sources4
Beta strandi674 – 676Combined sources3
Helixi692 – 697Combined sources6
Beta strandi700 – 702Combined sources3
Helixi703 – 708Combined sources6
Beta strandi719 – 721Combined sources3
Beta strandi730 – 736Combined sources7
Helixi744 – 751Combined sources8
Helixi754 – 763Combined sources10
Beta strandi777 – 779Combined sources3
Turni780 – 782Combined sources3
Helixi788 – 804Combined sources17
Helixi806 – 812Combined sources7
Beta strandi823 – 827Combined sources5
Beta strandi830 – 834Combined sources5
Beta strandi840 – 847Combined sources8
Helixi857 – 859Combined sources3
Beta strandi868 – 872Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7SX-ray1.80A28-885[»]
1C7TX-ray1.90A28-885[»]
1QBAX-ray1.85A28-885[»]
1QBBX-ray2.00A28-885[»]
ProteinModelPortaliQ54468.
SMRiQ54468.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ54468.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 20 family.Curated

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.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR015883. Glyco_hydro_20_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF03173. CHB_HEX. 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

« Hide

        10         20         30         40         50
MNAFKLSALA RLTATMGFLG GMGSAMADQQ LVDQLSQLKL NVKMLDNRAG
60 70 80 90 100
ENGVDCAALG ADWASCNRVL FTLSNDGQAI DGKDWVIYFH SPRQTLRVDN
110 120 130 140 150
DQFKIAHLTG DLYKLEPTAK FSGFPAGKAV EIPVVAEYWQ LFRNDFLPRW
160 170 180 190 200
YATSGDAKPK MLANTDTENL DQFVAPFTGD QWKRTKDDKN ILMTPASRFV
210 220 230 240 250
SNADLQTLPA GALRGKIVPT PMQVKVHAQD ADLRKGVALD LSTLVKPAAD
260 270 280 290 300
VVSQRFALLG VPVQTNGYPI KTDIQPGKFK GAMAVSGAYE LKIGKKEAQV
310 320 330 340 350
IGFDQAGVFY GLQSILSLVP SDGSGKIATL DASDAPRFPY RGIFLDVARN
360 370 380 390 400
FHKKDAVLRL LDQMAAYKLN KFHFHLSDDE GWRIEIPGLP ELTEVGGQRC
410 420 430 440 450
HDLSETTCLL PQYGQGPDVY GGFFSRQDYI DIIKYAQARQ IEVIPEIDMP
460 470 480 490 500
AHARAAVVSM EARYKKLHAA GKEQEANEFR LVDPTDTSNT TSVQFFNRQS
510 520 530 540 550
YLNPCLDSSQ RFVDKVIGEI AQMHKEAGQP IKTWHFGGDE AKNIRLGAGY
560 570 580 590 600
TDKAKPEPGK GIIDQSNEDK PWAKSQVCQT MIKEGKVADM EHLPSYFGQE
610 620 630 640 650
VSKLVKAHGI DRMQAWQDGL KDAESSKAFA TSRVGVNFWD TLYWGGFDSV
660 670 680 690 700
NDWANKGYEV VVSNPDYVYM DFPYEVNPDE RGYYWGTRFS DERKVFSFAP
710 720 730 740 750
DNMPQNAETS VDRDGNHFNA KSDKPWPGAY GLSAQLWSET QRTDPQMEYM
760 770 780 790 800
IFPRALSVAE RSWHRAGWEQ DYRAGREYKG GETHFVDTQA LEKDWLRFAN
810 820 830 840 850
ILGQRELAKL DKGGVAYRLP VPGARVAAGK LEANIALPGL GIEYSTDGGK
860 870 880
QWQRYDAKAK PAVSGEVQVR SVSPDGKRYS RAEKV
Length:885
Mass (Da):98,548
Last modified:November 1, 1996 - v1
Checksum:iA749CC0F507DE2E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43594 Genomic DNA. Translation: AAB03808.1.
PIRiJC4732.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L43594 Genomic DNA. Translation: AAB03808.1.
PIRiJC4732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C7SX-ray1.80A28-885[»]
1C7TX-ray1.90A28-885[»]
1QBAX-ray1.85A28-885[»]
1QBBX-ray2.00A28-885[»]
ProteinModelPortaliQ54468.
SMRiQ54468.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00349.
BioCyciMetaCyc:MONOMER-17688.

Miscellaneous databases

EvolutionaryTraceiQ54468.

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.
IPR029018. Chitobiase/Hex_dom_2-like.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR015883. Glyco_hydro_20_cat.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
IPR014756. Ig_E-set.
[Graphical view]
PfamiPF03173. CHB_HEX. 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.
ProtoNetiSearch...

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: November 2, 2016
This is version 109 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

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.