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Q0TR53 (OGA_CLOP1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
O-GlcNAcase nagJ
EC=3.2.1.169
Alternative name(s):
Beta-N-acetylhexosaminidase
Beta-hexosaminidase
GH84
Hexosaminidase B
N-acetyl-beta-glucosaminidase
Gene names
Name:nagJ
Ordered Locus Names:CPF_1442
OrganismClostridium perfringens (strain ATCC 13124 / NCTC 8237 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195103 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length1001 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.

Catalytic activity

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.

Enzyme regulation

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

Subunit structure

Homodimer. Ref.2

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 84 family.

Contains 1 fibronectin type-III domain.

Biophysicochemical properties

Kinetic parameters:

KM=2.9 µM for 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide (4MU-NAG) Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 1001971O-GlcNAcase nagJ
PRO_0000257985

Regions

Domain913 – 99987Fibronectin type-III
Region179 – 469291Catalytic domain
Region394 – 4018Substrate binding
Coiled coil515 – 54329 Potential
Coiled coil573 – 59725 Potential

Sites

Active site2181 Potential Ref.2
Active site2971 Ref.2
Active site2981Proton donor Probable Ref.2
Binding site1871Substrate; via carbonyl oxygen Ref.2
Binding site3351Substrate By similarity Ref.2
Binding site4291Substrate Ref.2
Site3351Transition state stabilizer Potential

Experimental info

Mutagenesis2971D → A: 99% decrease in activity for 4MU-NAG. Ref.2
Mutagenesis2981D → N: 99% decrease in activity for 4MU-NAG. Ref.2
Mutagenesis3351Y → F: 99% decrease in activity for 4MU-NAG. Ref.2
Mutagenesis3901N → A: No change in activity for 4MU-NAG. Ref.2
Mutagenesis3961N → A: 99% decrease in activity for 4MU-NAG. Ref.2
Mutagenesis4011D → A: 99% decrease in activity for 4MU-NAG. Ref.2
Mutagenesis4901W → A: 97% decrease in activity for 4MU-NAG. Ref.2

Secondary structure

1 ............................................................................................................. 1001
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q0TR53 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 3B918C7DB544A2DC

FASTA1,001111,080
        10         20         30         40         50         60 
MKRKMLKRLL TSAFACMFIA NGLITTTVRA VGPKTGEENQ VLVPNLNPTP ENLEVVGDGF 

        70         80         90        100        110        120 
KITSSINLVG EEEADENAVN ALREFLTANN IEINSENDPN STTLIIGEVD DDIPELDEAL 

       130        140        150        160        170        180 
NGTTAENLKE EGYALVSNDG KIAIEGKDGD GTFYGVQTFK QLVKESNIPE VNITDYPTVS 

       190        200        210        220        230        240 
ARGIVEGFYG TPWTHQDRLD QIKFYGENKL NTYIYAPKDD PYHREKWREP YPESEMQRMQ 

       250        260        270        280        290        300 
ELINASAENK VDFVFGISPG IDIRFDGDAG EEDFNHLITK AESLYDMGVR SFAIYWDDIQ 

       310        320        330        340        350        360 
DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRAYT RIFAETVDPS 

       370        380        390        400        410        420 
IEVMWTGPGV VTNEIPLSDA QLISGIYNRN MAVWWNYPVT DYFKGKLALG PMHGLDKGLN 

       430        440        450        460        470        480 
QYVDFFTVNP MEHAELSKIS IHTAADYSWN MDNYDYDKAW NRAIDMLYGD LAEDMKVFAN 

       490        500        510        520        530        540 
HSTRMDNKTW AKSGREDAPE LRAKMDELWN KLSSKEDASA LIEELYGEFA RMEEACNNLK 

       550        560        570        580        590        600 
ANLPEVALEE CSRQLDELIT LAQGDKASLD MIVAQLNEDT EAYESAKEIA QNKLNTALSS 

       610        620        630        640        650        660 
FAVISEKVAQ SFIQEALSFD LTLINPRTVK ITASSEETSG ENAPASFASD GDMNTFWHSK 

       670        680        690        700        710        720 
WSSPAHEGPH HLTLELDNVY EINKVKYAPR QDSKNGRITG YKVSVSLDGE NFTEVKTGTL 

       730        740        750        760        770        780 
EDNAAIKFIE FDSVDAKYVR LDVTDSVSDQ ANGRGKFATA AEVNVHGKLK ENAEVTGSVS 

       790        800        810        820        830        840 
LEALEEVQVG ENLEVGVGID ELVNAEAFAY DFTLNYDENA FEYVEAISDD GVFVNAKKIE 

       850        860        870        880        890        900 
DGKVRVLVSS LTGEPLPAKE VLAKVVLRAE AKAEGSNLSV TNSSVGDGEG LVHEIAGTEK 

       910        920        930        940        950        960 
TVNIIEGTSP EIVVNPVRDF KASEINKKNV TVTWTEPETT EGLEGYILYK DGKKVAEIGK 

       970        980        990       1000 
DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA R

« Hide

References

« Hide 'large scale' references
[1]"Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens."
Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Khouri H. expand/collapse author list , Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B., Paulsen I.T.
Genome Res. 16:1031-1040(2006) [PubMed: 16825665] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13124 / NCTC 8237 / Type A.
[2]"Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis."
Rao F.V., Dorfmueller H.C., Villa F., Allwood M., Eggleston I.M., van Aalten D.M.
EMBO J. 25:1569-1578(2006) [PubMed: 16541109] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 31-624 IN COMPLEX WITH INHIBITOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-297; ASP-298; TYR-335; ASN-390; ASN-396; ASP-401 AND TRP-490.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000246 Genomic DNA. Translation: ABG84519.1.
RefSeqYP_695887.1. NC_008261.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CBIX-ray2.25A/B31-624[»]
2CBJX-ray2.35A/B31-624[»]
2J62X-ray2.26A/B31-624[»]
2JH2X-ray2.50A/B/C768-909[»]
2O4ENMR-A768-909[»]
2OZNX-ray1.60A768-909[»]
2V5DX-ray3.30A31-767[»]
2WB5X-ray2.31A/B31-624[»]
2X0YX-ray2.25A/B31-624[»]
2XPKX-ray2.40A/B31-624[»]
ProteinModelPortalQ0TR53.
SMRQ0TR53. Positions 40-767, 774-907.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0TR53.

Protein family/group databases

CAZyCBM32. Carbohydrate-Binding Module Family 32.
GH84. Glycoside Hydrolase Family 84.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4202790.
GenomeReviewsGene locus CPF_1442 in contig CP000246_GR.
KEGGcpf:CPF_1442.
PATRIC19485150. VBICloPer106549_1395.
TIGRCPF_1442.

Phylogenomic databases

eggNOGNOG69445.
HOGENOMHBG061512.
OMAEVALEEC.
ProtClustDBCLSK518842.

Enzyme and pathway databases

BioCycCPER195103:CPF_1442-MONOMER.

Family and domain databases

InterProIPR015882. Acetylhexosaminidase_sua/b.
IPR011496. Beta-N-acetylglucosaminidase.
IPR008965. Carb-bd_dom.
IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR018452. Cohesin_dom_subgr.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
[Graphical view]
Gene3DG3DSA:2.60.40.680. Cohesin. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
KOK01197.
PfamPF00754. F5_F8_type_C. 1 hit.
PF00041. fn3. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
PF07555. NAGidase. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMSSF49384. Cellul_bind. 1 hit.
SSF49265. FN_III-like. 1 hit.
SSF49785. Gal_bind_like. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
PROSITEPS50853. FN3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOGA_CLOP1
AccessionPrimary (citable) accession number: Q0TR53
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents