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Protein

O-GlcNAcase NagJ

Gene

nagJ

Organism
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds carbohydrates (PubMed:16990278). Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.3 Publications

Catalytic activityi

[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.3 Publications
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.3 Publications
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.2 Publications

Enzyme regulationi

Inhibited by O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc) and streptozotocin.2 Publications

Kineticsi

  1. KM=2.9 µM for 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide (4MU-NAG)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei187 – 1871Substrate; via carbonyl oxygen1 Publication
    Binding sitei218 – 2181Substrate1 Publication
    Binding sitei297 – 2971Substrate1 Publication
    Active sitei298 – 2981Proton donor1 Publication
    Binding sitei335 – 3351Substrate1 Publication
    Binding sitei401 – 4011Substrate1 Publication
    Binding sitei429 – 4291Substrate1 Publication

    GO - Molecular functioni

    • beta-N-acetylglucosaminidase activity Source: UniProtKB
    • carbohydrate binding Source: UniProtKB

    GO - Biological processi

    • carbohydrate metabolic process Source: UniProtKB
    • protein deglycosylation Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciCPER195103:GHAW-1460-MONOMER.
    BRENDAi3.2.1.169. 1503.

    Protein family/group databases

    CAZyiCBM32. Carbohydrate-Binding Module Family 32.
    GH84. Glycoside Hydrolase Family 84.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    O-GlcNAcase NagJ (EC:3.2.1.1693 Publications)
    Alternative name(s):
    Beta-N-acetylglucosaminidase (EC:3.2.1.522 Publications)
    Beta-N-acetylhexosaminidase
    Beta-hexosaminidase
    GH84C1 Publication
    Hexosaminidase B
    N-acetyl-beta-D-glucosaminidase
    Gene namesi
    Name:nagJ
    Ordered Locus Names:CPF_1442
    OrganismiClostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
    Taxonomic identifieri195103 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
    Proteomesi
    • UP000001823 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi297 – 2971D → A: 99% decrease in activity for 4MU-NAG. 1 Publication
    Mutagenesisi298 – 2981D → N: 99% decrease in activity for 4MU-NAG. 2 Publications
    Mutagenesisi335 – 3351Y → F: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication
    Mutagenesisi390 – 3901N → A: No change in activity for 4MU-NAG. 1 Publication
    Mutagenesisi396 – 3961N → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication
    Mutagenesisi401 – 4011D → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication
    Mutagenesisi490 – 4901W → A: Strongly decreases affinity for 4MU-NAG. 97% decrease in activity for 4MU-NAG. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence analysisAdd
    BLAST
    Chaini31 – 1001971O-GlcNAcase NagJPRO_0000257985Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi195103.CPF_1442.

    Structurei

    Secondary structure

    1
    1001
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi51 – 555Combined sources
    Beta strandi64 – 707Combined sources
    Turni71 – 733Combined sources
    Helixi76 – 8813Combined sources
    Beta strandi95 – 973Combined sources
    Beta strandi101 – 1088Combined sources
    Beta strandi109 – 1113Combined sources
    Helixi114 – 1207Combined sources
    Beta strandi133 – 1386Combined sources
    Beta strandi141 – 1488Combined sources
    Helixi149 – 16214Combined sources
    Beta strandi164 – 1685Combined sources
    Beta strandi171 – 1755Combined sources
    Beta strandi178 – 1858Combined sources
    Beta strandi189 – 1913Combined sources
    Helixi195 – 20713Combined sources
    Beta strandi212 – 2154Combined sources
    Helixi221 – 2233Combined sources
    Turni224 – 2285Combined sources
    Helixi233 – 2353Combined sources
    Helixi236 – 24813Combined sources
    Beta strandi252 – 2576Combined sources
    Helixi259 – 2613Combined sources
    Helixi268 – 28518Combined sources
    Turni286 – 2883Combined sources
    Beta strandi291 – 2955Combined sources
    Helixi304 – 31714Combined sources
    Helixi319 – 3224Combined sources
    Beta strandi323 – 3253Combined sources
    Beta strandi329 – 3313Combined sources
    Helixi337 – 3404Combined sources
    Beta strandi341 – 3466Combined sources
    Helixi348 – 3569Combined sources
    Beta strandi361 – 3655Combined sources
    Beta strandi367 – 3715Combined sources
    Helixi377 – 38711Combined sources
    Beta strandi391 – 3955Combined sources
    Helixi419 – 4213Combined sources
    Beta strandi423 – 4286Combined sources
    Helixi434 – 44916Combined sources
    Helixi451 – 4533Combined sources
    Helixi456 – 46813Combined sources
    Helixi469 – 4713Combined sources
    Helixi472 – 4798Combined sources
    Beta strandi488 – 4903Combined sources
    Beta strandi492 – 4954Combined sources
    Helixi499 – 51214Combined sources
    Turni513 – 5153Combined sources
    Helixi519 – 54224Combined sources
    Helixi545 – 57632Combined sources
    Helixi580 – 59920Combined sources
    Turni606 – 6083Combined sources
    Helixi609 – 61810Combined sources
    Helixi621 – 6233Combined sources
    Beta strandi628 – 6347Combined sources
    Beta strandi639 – 6413Combined sources
    Helixi645 – 6484Combined sources
    Beta strandi649 – 6513Combined sources
    Beta strandi662 – 6643Combined sources
    Beta strandi671 – 68818Combined sources
    Beta strandi697 – 71923Combined sources
    Beta strandi722 – 7254Combined sources
    Beta strandi727 – 74721Combined sources
    Beta strandi749 – 7524Combined sources
    Turni754 – 7563Combined sources
    Beta strandi759 – 7668Combined sources
    Beta strandi776 – 7827Combined sources
    Beta strandi785 – 7884Combined sources
    Beta strandi792 – 80413Combined sources
    Beta strandi808 – 8158Combined sources
    Turni818 – 8203Combined sources
    Beta strandi821 – 8277Combined sources
    Beta strandi832 – 8409Combined sources
    Beta strandi843 – 85412Combined sources
    Beta strandi858 – 86912Combined sources
    Beta strandi873 – 88614Combined sources
    Beta strandi888 – 8903Combined sources
    Beta strandi892 – 8943Combined sources
    Beta strandi898 – 9058Combined sources
    Beta strandi918 – 9258Combined sources
    Beta strandi930 – 9356Combined sources
    Beta strandi943 – 9508Combined sources
    Beta strandi953 – 9597Combined sources
    Beta strandi964 – 9674Combined sources
    Beta strandi975 – 98410Combined sources
    Beta strandi993 – 9986Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CBIX-ray2.25A/B31-624[»]
    2CBJX-ray2.35A/B31-624[»]
    2J1AX-ray1.49A625-767[»]
    2J1EX-ray2.40A625-767[»]
    2J62X-ray2.26A/B31-624[»]
    2J7MX-ray2.30A625-767[»]
    2JH2X-ray2.50A/B/C768-909[»]
    2O4ENMR-A768-909[»]
    2OZNX-ray1.60A768-909[»]
    2V5CX-ray2.10A/B31-624[»]
    2V5DX-ray3.30A31-767[»]
    2VURX-ray2.20A/B31-624[»]
    2W1NX-ray1.80A765-1001[»]
    2WB5X-ray2.31A/B31-624[»]
    2X0YX-ray2.25A/B31-624[»]
    2XPKX-ray2.40A/B31-624[»]
    2YDQX-ray2.60A31-618[»]
    2YDRX-ray2.75A31-618[»]
    2YDSX-ray2.55A31-618[»]
    4ZXLX-ray2.60A39-617[»]
    ProteinModelPortaliQ0TR53.
    SMRiQ0TR53. Positions 40-767, 774-907.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0TR53.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini916 – 100186Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni179 – 469291Catalytic domainSequence analysisAdd
    BLAST
    Regioni394 – 3963Substrate binding1 Publication

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili515 – 54329Sequence analysisAdd
    BLAST
    Coiled coili573 – 59725Sequence analysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 84 family.Sequence analysis
    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Signal

    Phylogenomic databases

    eggNOGiENOG4105CPE. Bacteria.
    ENOG410XPBQ. LUCA.
    HOGENOMiHOG000052598.
    KOiK01197.
    OMAiARMEEAC.
    OrthoDBiPOG091H0IJT.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR011496. Beta-N-acetylglucosaminidase.
    IPR008965. Carb-bd_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR000421. FA58C.
    IPR003961. FN3_dom.
    IPR008979. Galactose-bd-like.
    IPR017853. Glycoside_hydrolase_SF.
    IPR015882. HEX_bac_N.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF00041. fn3. 1 hit.
    PF02838. Glyco_hydro_20b. 1 hit.
    PF07555. NAGidase. 1 hit.
    [Graphical view]
    SMARTiSM00060. FN3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF49384. SSF49384. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    PROSITEiPS50853. FN3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q0TR53-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKRKMLKRLL TSAFACMFIA NGLITTTVRA VGPKTGEENQ VLVPNLNPTP
    60 70 80 90 100
    ENLEVVGDGF KITSSINLVG EEEADENAVN ALREFLTANN IEINSENDPN
    110 120 130 140 150
    STTLIIGEVD DDIPELDEAL NGTTAENLKE EGYALVSNDG KIAIEGKDGD
    160 170 180 190 200
    GTFYGVQTFK QLVKESNIPE VNITDYPTVS ARGIVEGFYG TPWTHQDRLD
    210 220 230 240 250
    QIKFYGENKL NTYIYAPKDD PYHREKWREP YPESEMQRMQ ELINASAENK
    260 270 280 290 300
    VDFVFGISPG IDIRFDGDAG EEDFNHLITK AESLYDMGVR SFAIYWDDIQ
    310 320 330 340 350
    DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRAYT
    360 370 380 390 400
    RIFAETVDPS IEVMWTGPGV VTNEIPLSDA QLISGIYNRN MAVWWNYPVT
    410 420 430 440 450
    DYFKGKLALG PMHGLDKGLN QYVDFFTVNP MEHAELSKIS IHTAADYSWN
    460 470 480 490 500
    MDNYDYDKAW NRAIDMLYGD LAEDMKVFAN HSTRMDNKTW AKSGREDAPE
    510 520 530 540 550
    LRAKMDELWN KLSSKEDASA LIEELYGEFA RMEEACNNLK ANLPEVALEE
    560 570 580 590 600
    CSRQLDELIT LAQGDKASLD MIVAQLNEDT EAYESAKEIA QNKLNTALSS
    610 620 630 640 650
    FAVISEKVAQ SFIQEALSFD LTLINPRTVK ITASSEETSG ENAPASFASD
    660 670 680 690 700
    GDMNTFWHSK WSSPAHEGPH HLTLELDNVY EINKVKYAPR QDSKNGRITG
    710 720 730 740 750
    YKVSVSLDGE NFTEVKTGTL EDNAAIKFIE FDSVDAKYVR LDVTDSVSDQ
    760 770 780 790 800
    ANGRGKFATA AEVNVHGKLK ENAEVTGSVS LEALEEVQVG ENLEVGVGID
    810 820 830 840 850
    ELVNAEAFAY DFTLNYDENA FEYVEAISDD GVFVNAKKIE DGKVRVLVSS
    860 870 880 890 900
    LTGEPLPAKE VLAKVVLRAE AKAEGSNLSV TNSSVGDGEG LVHEIAGTEK
    910 920 930 940 950
    TVNIIEGTSP EIVVNPVRDF KASEINKKNV TVTWTEPETT EGLEGYILYK
    960 970 980 990 1000
    DGKKVAEIGK DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA

    R
    Length:1,001
    Mass (Da):111,080
    Last modified:September 5, 2006 - v1
    Checksum:i3B918C7DB544A2DC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000246 Genomic DNA. Translation: ABG84519.1.
    RefSeqiWP_003456570.1. NC_008261.1.

    Genome annotation databases

    EnsemblBacteriaiABG84519; ABG84519; CPF_1442.
    KEGGicpf:CPF_1442.
    PATRICi19485150. VBICloPer106549_1395.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000246 Genomic DNA. Translation: ABG84519.1.
    RefSeqiWP_003456570.1. NC_008261.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CBIX-ray2.25A/B31-624[»]
    2CBJX-ray2.35A/B31-624[»]
    2J1AX-ray1.49A625-767[»]
    2J1EX-ray2.40A625-767[»]
    2J62X-ray2.26A/B31-624[»]
    2J7MX-ray2.30A625-767[»]
    2JH2X-ray2.50A/B/C768-909[»]
    2O4ENMR-A768-909[»]
    2OZNX-ray1.60A768-909[»]
    2V5CX-ray2.10A/B31-624[»]
    2V5DX-ray3.30A31-767[»]
    2VURX-ray2.20A/B31-624[»]
    2W1NX-ray1.80A765-1001[»]
    2WB5X-ray2.31A/B31-624[»]
    2X0YX-ray2.25A/B31-624[»]
    2XPKX-ray2.40A/B31-624[»]
    2YDQX-ray2.60A31-618[»]
    2YDRX-ray2.75A31-618[»]
    2YDSX-ray2.55A31-618[»]
    4ZXLX-ray2.60A39-617[»]
    ProteinModelPortaliQ0TR53.
    SMRiQ0TR53. Positions 40-767, 774-907.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi195103.CPF_1442.

    Protein family/group databases

    CAZyiCBM32. Carbohydrate-Binding Module Family 32.
    GH84. Glycoside Hydrolase Family 84.

    Protocols and materials databases

    DNASUi4202790.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABG84519; ABG84519; CPF_1442.
    KEGGicpf:CPF_1442.
    PATRICi19485150. VBICloPer106549_1395.

    Phylogenomic databases

    eggNOGiENOG4105CPE. Bacteria.
    ENOG410XPBQ. LUCA.
    HOGENOMiHOG000052598.
    KOiK01197.
    OMAiARMEEAC.
    OrthoDBiPOG091H0IJT.

    Enzyme and pathway databases

    BioCyciCPER195103:GHAW-1460-MONOMER.
    BRENDAi3.2.1.169. 1503.

    Miscellaneous databases

    EvolutionaryTraceiQ0TR53.

    Family and domain databases

    Gene3Di2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR011496. Beta-N-acetylglucosaminidase.
    IPR008965. Carb-bd_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR000421. FA58C.
    IPR003961. FN3_dom.
    IPR008979. Galactose-bd-like.
    IPR017853. Glycoside_hydrolase_SF.
    IPR015882. HEX_bac_N.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF00041. fn3. 1 hit.
    PF02838. Glyco_hydro_20b. 1 hit.
    PF07555. NAGidase. 1 hit.
    [Graphical view]
    SMARTiSM00060. FN3. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF49384. SSF49384. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    PROSITEiPS50853. FN3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiOGA_CLOP1
    AccessioniPrimary (citable) accession number: Q0TR53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: September 5, 2006
    Last modified: September 7, 2016
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Metal-binding observed in X-ray crystal structures is artifactual.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome

    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.