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Reviewed, UniProtKB/Swiss-Prot Q8XL08 (OGA_CLOPE)

Last modified May 5, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    O-GlcNAcase nagJ
    EC=3.2.1.52
Alternative name(s):
    Beta-hexosaminidase
    N-acetyl-beta-glucosaminidase
    Beta-N-acetylhexosaminidase
    Hexosaminidase B
    GH84
Gene names
Name: nagJ
Ordered Locus Names: CPE1234
OrganismClostridium perfringens [Complete proteome] [HAMAP]
Taxonomic identifier1502 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

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Protein attributes

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

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General annotation (Comments)

Function

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

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. UniProtKB Q0TR53

Enzyme regulation

Inhibited by O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc) By similarity. UniProtKB Q0TR53

Subunit structure

Homodimer By similarity. UniProtKB Q0TR53

Sequence similarities

Belongs to the glycosyl hydrolase 84 family.

Contains 1 fibronectin type-III domain.

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Ontologies

Keywords
   DomainCoiled coil
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: InterPro

metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbeta-N-acetylhexosaminidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 1001971O-GlcNAcase nagJ
PRO_0000257986

Regions

Domain913 – 99987Fibronectin type-III
Region179 – 469291Catalytic domain By similarity UniProtKB Q0TR53
Region297 – 2982Substrate binding By similarity UniProtKB Q0TR53
Coiled coil515 – 54329 Potential
Coiled coil573 – 59725 Potential

Sites

Active site2181 Potential UniProtKB Q0TR53
Active site2971 By similarity UniProtKB Q0TR53
Active site2981Proton donor Probable UniProtKB Q0TR53
Binding site1871Substrate; via carbonyl oxygen By similarity UniProtKB Q0TR53
Binding site1891Substrate By similarity UniProtKB Q0TR53
Binding site2181Substrate By similarity UniProtKB Q0TR53
Binding site3351Substrate By similarity UniProtKB Q0TR53
Binding site3701Substrate By similarity UniProtKB Q0TR53
Binding site3941Substrate By similarity UniProtKB Q0TR53
Binding site3961Substrate By similarity UniProtKB Q0TR53
Binding site4011Substrate By similarity UniProtKB Q0TR53
Binding site4291Substrate By similarity UniProtKB Q0TR53
Site3351Transition state stabilizer Potential

Secondary structure

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

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q8XL08-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: E0C0A1575073946E

FASTA1,001111,109
        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 TPWTHKDRLD QIKFYGENKL NTYIYAPKDD PYHREKWREP YPENEMQRMQ 

       250        260        270        280        290        300 
ELIDASAENK VDFVFGISPG IDIRFDGEAG EEDFNHLIAK AESLYDMGVR SFAIYWDDIQ 

       310        320        330        340        350        360 
DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRTYT 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 EAAEVTGSVS 

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

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

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

       970        980        990       1000 
DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA R

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References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.
+Additional computationally mapped references.

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Cross-references

Sequence databases

BA000016 Genomic DNA. Translation: BAB80940.1.
RefSeqNP_562150.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2CBIX-ray2.25A/B31-624[»]
2CBJX-ray2.35A/B31-624[»]
2J1AX-ray1.49A625-767[»]
2J1EX-ray2.40A625-767[»]
2J62X-ray2.26A31-624[»]
2J7MX-ray2.30A625-767[»]
2V5CX-ray2.10A/B31-624[»]
2VURX-ray2.20A/B31-624[»]
2W1NX-ray1.80A765-1001[»]
ModBaseSearch...

Protein family/group databases

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

Genome annotation databases

GeneID989543.
GenomeReviewsGene locus CPE1234 in contig BA000016_GR.
KEGGcpe:CPE1234.
NMPDRfig|195102.1.peg.1297.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8XL08.
OMAQ8XL08. ITSSINL.

Enzyme and pathway databases

BioCycCPER195102:CPE1234-MON.
BRENDA3.2.1.52. 2406.

Family and domain databases

InterProIPR011496. Beta-N-acetylglucosaminidase.
IPR000421. Coagulation_factor_5/8-type_C.
IPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 1 hit.
PfamPF00754. F5_F8_type_C. 1 hit.
PF00041. fn3. 1 hit.
PF07555. NAGidase. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
[Graphical view]
PROSITEPS50853. FN3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameOGA_CLOPE
AccessionPrimary (citable) accession number: Q8XL08
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2002
Last modified: May 5, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents