Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Binding sitei187Substrate; via carbonyl oxygen1 Publication1
    Binding sitei218Substrate1 Publication1
    Binding sitei297Substrate1 Publication1
    Active sitei298Proton donor1 Publication1
    Binding sitei335Substrate1 Publication1
    Binding sitei401Substrate1 Publication1
    Binding sitei429Substrate1 Publication1

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi297D → A: 99% decrease in activity for 4MU-NAG. 1 Publication1
    Mutagenesisi298D → N: 99% decrease in activity for 4MU-NAG. 2 Publications1
    Mutagenesisi335Y → F: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication1
    Mutagenesisi390N → A: No change in activity for 4MU-NAG. 1 Publication1
    Mutagenesisi396N → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication1
    Mutagenesisi401D → A: Strongly decreases affinity for 4MU-NAG. 99% decrease in activity for 4MU-NAG. 1 Publication1
    Mutagenesisi490W → A: Strongly decreases affinity for 4MU-NAG. 97% decrease in activity for 4MU-NAG. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 30Sequence analysisAdd BLAST30
    ChainiPRO_000025798531 – 1001O-GlcNAcase NagJAdd BLAST971

    Interactioni

    Protein-protein interaction databases

    STRINGi195103.CPF_1442.

    Structurei

    Secondary structure

    11001
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi51 – 55Combined sources5
    Beta strandi64 – 70Combined sources7
    Turni71 – 73Combined sources3
    Helixi76 – 88Combined sources13
    Beta strandi95 – 97Combined sources3
    Beta strandi101 – 108Combined sources8
    Beta strandi109 – 111Combined sources3
    Helixi114 – 120Combined sources7
    Beta strandi133 – 138Combined sources6
    Beta strandi141 – 148Combined sources8
    Helixi149 – 162Combined sources14
    Beta strandi164 – 168Combined sources5
    Beta strandi171 – 175Combined sources5
    Beta strandi178 – 185Combined sources8
    Beta strandi189 – 191Combined sources3
    Helixi195 – 207Combined sources13
    Beta strandi212 – 215Combined sources4
    Helixi221 – 223Combined sources3
    Turni224 – 228Combined sources5
    Helixi233 – 235Combined sources3
    Helixi236 – 248Combined sources13
    Beta strandi252 – 257Combined sources6
    Helixi259 – 261Combined sources3
    Helixi268 – 285Combined sources18
    Turni286 – 288Combined sources3
    Beta strandi291 – 295Combined sources5
    Helixi304 – 317Combined sources14
    Helixi319 – 322Combined sources4
    Beta strandi323 – 325Combined sources3
    Beta strandi329 – 331Combined sources3
    Helixi337 – 340Combined sources4
    Beta strandi341 – 346Combined sources6
    Helixi348 – 356Combined sources9
    Beta strandi361 – 365Combined sources5
    Beta strandi367 – 371Combined sources5
    Helixi377 – 387Combined sources11
    Beta strandi391 – 395Combined sources5
    Helixi419 – 421Combined sources3
    Beta strandi423 – 428Combined sources6
    Helixi434 – 449Combined sources16
    Helixi451 – 453Combined sources3
    Helixi456 – 468Combined sources13
    Helixi469 – 471Combined sources3
    Helixi472 – 479Combined sources8
    Beta strandi488 – 490Combined sources3
    Beta strandi492 – 495Combined sources4
    Helixi499 – 512Combined sources14
    Turni513 – 515Combined sources3
    Helixi519 – 542Combined sources24
    Helixi545 – 576Combined sources32
    Helixi580 – 599Combined sources20
    Turni606 – 608Combined sources3
    Helixi609 – 618Combined sources10
    Helixi621 – 623Combined sources3
    Beta strandi628 – 634Combined sources7
    Beta strandi639 – 641Combined sources3
    Helixi645 – 648Combined sources4
    Beta strandi649 – 651Combined sources3
    Beta strandi662 – 664Combined sources3
    Beta strandi671 – 688Combined sources18
    Beta strandi697 – 719Combined sources23
    Beta strandi722 – 725Combined sources4
    Beta strandi727 – 747Combined sources21
    Beta strandi749 – 752Combined sources4
    Turni754 – 756Combined sources3
    Beta strandi759 – 766Combined sources8
    Beta strandi776 – 782Combined sources7
    Beta strandi785 – 788Combined sources4
    Beta strandi792 – 804Combined sources13
    Beta strandi808 – 815Combined sources8
    Turni818 – 820Combined sources3
    Beta strandi821 – 827Combined sources7
    Beta strandi832 – 840Combined sources9
    Beta strandi843 – 854Combined sources12
    Beta strandi858 – 869Combined sources12
    Beta strandi873 – 886Combined sources14
    Beta strandi888 – 890Combined sources3
    Beta strandi892 – 894Combined sources3
    Beta strandi898 – 905Combined sources8
    Beta strandi918 – 925Combined sources8
    Beta strandi930 – 935Combined sources6
    Beta strandi943 – 950Combined sources8
    Beta strandi953 – 959Combined sources7
    Beta strandi964 – 967Combined sources4
    Beta strandi975 – 984Combined sources10
    Beta strandi993 – 998Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0TR53.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini916 – 1001Fibronectin type-IIIPROSITE-ProRule annotationAdd BLAST86

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni179 – 469Catalytic domainSequence analysisAdd BLAST291
    Regioni394 – 396Substrate binding1 Publication3

    Coiled coil

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Coiled coili515 – 543Sequence analysisAdd BLAST29
    Coiled coili573 – 597Sequence analysisAdd BLAST25

    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

    CDDicd00063. FN3. 1 hit.
    Gene3Di2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    2.60.40.680. 1 hit.
    3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR011496. Beta-N-acetylglucosaminidase.
    IPR008965. Carb-bd_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR002102. Cohesin_dom.
    IPR000421. FA58C.
    IPR003961. FN3_dom.
    IPR008979. Galactose-bd-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    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
    PDB 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.
    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

    BRENDAi3.2.1.169. 1503.

    Miscellaneous databases

    EvolutionaryTraceiQ0TR53.

    Family and domain databases

    CDDicd00063. FN3. 1 hit.
    Gene3Di2.60.120.260. 1 hit.
    2.60.40.10. 1 hit.
    2.60.40.680. 1 hit.
    3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR011496. Beta-N-acetylglucosaminidase.
    IPR008965. Carb-bd_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR002102. Cohesin_dom.
    IPR000421. FA58C.
    IPR003961. FN3_dom.
    IPR008979. Galactose-bd-like.
    IPR013781. Glyco_hydro_catalytic_dom.
    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: November 30, 2016
    This is version 81 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.