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Q54468

- CHB_SERMA

UniProt

Q54468 - CHB_SERMA

Protein

Chitobiase

Gene

chb

Organism
Serratia marcescens
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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

    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.
    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

    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: October 1, 2014
    This is version 101 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