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Q8XL08 (OGA_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 74. 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:CPE1234
OrganismClostridium perfringens [Complete proteome] [HAMAP]
Taxonomic identifier1502 [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 By similarity.

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) 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.

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
Region394 – 4018Substrate binding By similarity
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 site3351Substrate By similarity UniProtKB Q0TR53
Binding site4291Substrate By similarity UniProtKB Q0TR53

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8XL08 [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

« Hide

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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000016 Genomic DNA. Translation: BAB80940.1.
RefSeqNP_562150.1. NC_003366.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ8XL08.
SMRQ8XL08. Positions 40-909.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-46266N.

Protein family/group databases

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

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID989543.
GenomeReviewsGene locus CPE1234 in contig BA000016_GR.
KEGGcpe:CPE1234.
NMPDRfig|195102.1.peg.1297.
PATRIC19496418. VBICloPer59675_1306.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG061512.
OMAEVALEEC.
ProtClustDBCLSK518842.

Enzyme and pathway databases

BioCycCPER195102:CPE1234-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_CLOPE
AccessionPrimary (citable) accession number: Q8XL08
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 74 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

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