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Protein

N,N'-diacetylchitobiose phosphorylase

Gene

chbP

Organism
Vibrio proteolyticus (Aeromonas proteolytica)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible phosphorolysis of chitobiose (N,N'-diacetylchitobiose or (GlcNAc)2) into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration.1 Publication

Catalytic activityi

N,N'-diacetylchitobiose + phosphate = N-acetyl-D-glucosamine + N-acetyl-alpha-D-glucosamine 1-phosphate.1 Publication

Kineticsi

  1. KM=2.0 mM for N,N'-diacetylchitobiose1 Publication
  2. KM=69 mM for alpha-D-glucosyl-(1-4)-2-acetamide-2-deoxy-D-glucose1 Publication
  3. KM=14 mM for N-acetyl-alpha-D-glucosamine 1-phosphate1 Publication
  4. KM=0.48 mM for alpha-D-glucose 1-phosphate1 Publication

    pH dependencei

    Optimum pH is 7.0-7.7.1 Publication

    Temperature dependencei

    Optimum temperature is 30 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi140 – 1401Calcium 31 Publication
    Metal bindingi186 – 1861Calcium 11 Publication
    Metal bindingi187 – 1871Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi190 – 1901Calcium 1; via carbonyl oxygen1 Publication
    Metal bindingi196 – 1961Calcium 1; via carbonyl oxygen1 Publication
    Binding sitei333 – 3331Substrate
    Binding sitei343 – 3431Substrate
    Active sitei489 – 4891NucleophileBy similarity
    Active sitei527 – 5271Proton donorBy similarity
    Binding sitei637 – 6371Substrate
    Binding sitei644 – 6441Substrate
    Binding sitei690 – 6901Substrate
    Metal bindingi791 – 7911Calcium 2; via carbonyl oxygen1 Publication
    Metal bindingi793 – 7931Calcium 21 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi2.4.1.280. 167.
    SABIO-RKQ76IQ9.

    Protein family/group databases

    CAZyiGH94. Glycoside Hydrolase Family 94.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N,N'-diacetylchitobiose phosphorylase (EC:2.4.1.280)
    Alternative name(s):
    Chitobiose phosphorylase
    Gene namesi
    Name:chbP
    OrganismiVibrio proteolyticus (Aeromonas proteolytica)
    Taxonomic identifieri671 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 801801N,N'-diacetylchitobiose phosphorylasePRO_0000424107Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    801
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75Combined sources
    Turni8 – 114Combined sources
    Beta strandi12 – 165Combined sources
    Beta strandi25 – 284Combined sources
    Beta strandi30 – 389Combined sources
    Beta strandi41 – 488Combined sources
    Turni50 – 523Combined sources
    Beta strandi61 – 644Combined sources
    Beta strandi66 – 683Combined sources
    Beta strandi70 – 756Combined sources
    Turni76 – 783Combined sources
    Beta strandi81 – 866Combined sources
    Turni87 – 904Combined sources
    Turni93 – 953Combined sources
    Beta strandi96 – 1038Combined sources
    Beta strandi106 – 1138Combined sources
    Beta strandi116 – 1238Combined sources
    Beta strandi128 – 13912Combined sources
    Beta strandi141 – 1433Combined sources
    Beta strandi145 – 1528Combined sources
    Helixi160 – 1645Combined sources
    Helixi167 – 1704Combined sources
    Beta strandi173 – 1797Combined sources
    Beta strandi182 – 1876Combined sources
    Turni193 – 1964Combined sources
    Beta strandi197 – 2048Combined sources
    Beta strandi207 – 2126Combined sources
    Helixi213 – 2175Combined sources
    Helixi227 – 2315Combined sources
    Beta strandi240 – 2423Combined sources
    Beta strandi244 – 25411Combined sources
    Beta strandi259 – 26911Combined sources
    Helixi272 – 2798Combined sources
    Helixi283 – 30119Combined sources
    Beta strandi304 – 3074Combined sources
    Helixi311 – 3177Combined sources
    Helixi320 – 33112Combined sources
    Beta strandi336 – 3383Combined sources
    Beta strandi345 – 3473Combined sources
    Helixi348 – 3547Combined sources
    Turni359 – 3613Combined sources
    Helixi363 – 37513Combined sources
    Beta strandi385 – 3873Combined sources
    Helixi389 – 3924Combined sources
    Helixi420 – 4223Combined sources
    Beta strandi424 – 4263Combined sources
    Helixi427 – 4304Combined sources
    Helixi431 – 44212Combined sources
    Helixi445 – 4495Combined sources
    Beta strandi451 – 4533Combined sources
    Beta strandi459 – 4613Combined sources
    Helixi462 – 47514Combined sources
    Beta strandi483 – 4864Combined sources
    Beta strandi489 – 4913Combined sources
    Beta strandi497 – 5015Combined sources
    Helixi502 – 52221Combined sources
    Helixi525 – 54521Combined sources
    Beta strandi546 – 5483Combined sources
    Turni549 – 5524Combined sources
    Beta strandi564 – 5663Combined sources
    Helixi577 – 5859Combined sources
    Helixi591 – 60515Combined sources
    Beta strandi613 – 6164Combined sources
    Turni623 – 6253Combined sources
    Helixi627 – 6304Combined sources
    Beta strandi640 – 6434Combined sources
    Helixi646 – 65510Combined sources
    Helixi659 – 66911Combined sources
    Helixi671 – 6744Combined sources
    Helixi678 – 6814Combined sources
    Beta strandi689 – 6924Combined sources
    Turni698 – 7014Combined sources
    Beta strandi703 – 7086Combined sources
    Helixi711 – 72111Combined sources
    Beta strandi726 – 7283Combined sources
    Beta strandi733 – 7353Combined sources
    Beta strandi745 – 7528Combined sources
    Beta strandi755 – 7628Combined sources
    Beta strandi771 – 7766Combined sources
    Beta strandi779 – 7813Combined sources
    Beta strandi783 – 7853Combined sources
    Beta strandi793 – 8008Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V7VX-ray1.80A1-801[»]
    1V7WX-ray1.60A1-801[»]
    1V7XX-ray2.00A1-801[»]
    ProteinModelPortaliQ76IQ9.
    SMRiQ76IQ9. Positions 1-801.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ76IQ9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni349 – 3502Substrate binding
    Regioni490 – 4923Substrate binding
    Regioni709 – 7102Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 94 family.Curated

    Phylogenomic databases

    KOiK18675.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    2.70.98.40. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR009342. Carb-bd_put_dom.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR033432. GH36_catalytic.
    IPR005196. Glyco_hydro_65_N.
    IPR010383. Glyco_hydrolase_94.
    [Graphical view]
    PfamiPF17167. Glyco_hydro_36. 1 hit.
    PF06165. Glyco_transf_36. 1 hit.
    [Graphical view]
    SMARTiSM01068. CBM_X. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    SSF74650. SSF74650. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q76IQ9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKYGYFDNDN REYVITRPDV PAPWTNYLGT EKFCTVISHN AGGYSFYNSP
    60 70 80 90 100
    EYNRVTKFRP NATFDRPGHY VYLRDDDSGD YWSISWQPVA KSLDEAQYQI
    110 120 130 140 150
    RHGLSYSKFQ CDYNGIHARK TLFVPKGEDA EIWDVVIKNT SDQVRTISAF
    160 170 180 190 200
    SFVEFSFSHI QSDNQNHQMS LYSAGTAYRP GLIEYDLYYN TDDFEGFYYL
    210 220 230 240 250
    ASTFDPDSYD GQRDRFLGLY RDEANPLAVE QGRCSNSAQT CYNHCGSLHK
    260 270 280 290 300
    QFTLQPGEEI RFAYILGIGK GNGERLREHY QDVANIDAAF AAIKAHWDER
    310 320 330 340 350
    CAKFQVKSPN QGLDTMINAW TLYQAETCVV WSRFASFIEV GGRTGLGYRD
    360 370 380 390 400
    TAQDAISVPH ANPEMTRKRI VDLLRGQVKA GYGLHLFDPD WFDPEKEDVA
    410 420 430 440 450
    PSKSPTVVPT PSDEDKIHGI KDTCSDDHLW LIPTICKYVM ETGETSFFDQ
    460 470 480 490 500
    MIPYADGGEA SVYEHMKAAL DFSAEYVGQT GICKGLRADW NDCLNLGGGE
    510 520 530 540 550
    SSMVSFLHFW ALQEFIDLAK FLGKDQDVNT YTEMAANVRE ACETHLWDDE
    560 570 580 590 600
    GGWYIRGLTK NGDKIGTAQQ QEGRVHLESN TLAVLSGLAS QERGEQAMDA
    610 620 630 640 650
    VDEHLFSPYG LHLNAPSFST PNDDIGFVTR VYQGVKENGA IFSHPNPWAW
    660 670 680 690 700
    VAETKLGRGD RAMKFYDALN PYNQNDIIEK RIAEPYSYVQ FIMGRDHQDH
    710 720 730 740 750
    GRANHPWLTG TSGWAYFAVT NYILGVQSGF TGLSVDPCIP SDWPGFEVTR
    760 770 780 790 800
    QWRGATYHIQ VENPDHVSKG VKSITLNGAP IQGRIPPQAQ GSDNQVVVVL

    G
    Length:801
    Mass (Da):90,361
    Last modified:July 5, 2004 - v1
    Checksum:iBB9D864E7FFB6EDC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB096684 Genomic DNA. Translation: BAC87867.1.

    Genome annotation databases

    KEGGiag:BAC87867.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB096684 Genomic DNA. Translation: BAC87867.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V7VX-ray1.80A1-801[»]
    1V7WX-ray1.60A1-801[»]
    1V7XX-ray2.00A1-801[»]
    ProteinModelPortaliQ76IQ9.
    SMRiQ76IQ9. Positions 1-801.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGH94. Glycoside Hydrolase Family 94.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:BAC87867.

    Phylogenomic databases

    KOiK18675.

    Enzyme and pathway databases

    BRENDAi2.4.1.280. 167.
    SABIO-RKQ76IQ9.

    Miscellaneous databases

    EvolutionaryTraceiQ76IQ9.

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    2.70.98.40. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR009342. Carb-bd_put_dom.
    IPR011013. Gal_mutarotase_SF_dom.
    IPR033432. GH36_catalytic.
    IPR005196. Glyco_hydro_65_N.
    IPR010383. Glyco_hydrolase_94.
    [Graphical view]
    PfamiPF17167. Glyco_hydro_36. 1 hit.
    PF06165. Glyco_transf_36. 1 hit.
    [Graphical view]
    SMARTiSM01068. CBM_X. 1 hit.
    [Graphical view]
    SUPFAMiSSF48208. SSF48208. 1 hit.
    SSF74650. SSF74650. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    1. "Reaction mechanism of chitobiose phosphorylase from Vibrio proteolyticus: identification of family 36 glycosyltransferase in Vibrio."
      Honda Y., Kitaoka M., Hayashi K.
      Biochem. J. 377:225-232(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "Chitobiose phosphorylase from Vibrio proteolyticus, a member of glycosyl transferase family 36, has a clan GH-L-like (alpha/alpha)(6) barrel fold."
      Hidaka M., Honda Y., Kitaoka M., Nirasawa S., Hayashi K., Wakagi T., Shoun H., Fushinobu S.
      Structure 12:937-947(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CALCIUM; 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE AND N-ACETYL-D-GLUCOSAMINE, SUBUNIT.

    Entry informationi

    Entry nameiCHBP_VIBPR
    AccessioniPrimary (citable) accession number: Q76IQ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 16, 2013
    Last sequence update: July 5, 2004
    Last modified: June 8, 2016
    This is version 53 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

    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.