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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: 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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
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.
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

« 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 .
PIRi JC4732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 103 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