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Protein

Protein O-GlcNAcase

Gene

OG2516_04129

Organism
Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves GlcNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrate (in vitro).1 Publication

Catalytic activityi

[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.1 Publication
[Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.1 Publication
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

Enzyme regulationi

Inhibited by PUGNac (O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate).1 Publication

Kineticsi

  1. KM=8.5 mM for p-nitrophenyl-GlcNAc1 Publication
  2. KM=2.9 mM for 4-methylumbelliferone-GlcNAc1 Publication

    pH dependencei

    Optimum pH is 7.4-7.6.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei8Substrate; via carbonyl oxygenImported1
    Binding sitei39SubstrateBy similarity1
    Binding sitei115SubstrateBy similarity1
    Active sitei116Proton donorBy similarity1
    Binding sitei160SubstrateImported1
    Binding sitei226SubstrateImported1
    Binding sitei254SubstrateImported1

    GO - Molecular functioni

    • beta-N-acetylglucosaminidase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH84. Glycoside Hydrolase Family 84.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein O-GlcNAcase1 Publication (EC:3.2.1.1691 Publication)
    Short name:
    OGA1 Publication
    Alternative name(s):
    Beta-N-acetylglucosaminidase (EC:3.2.1.521 Publication)
    Beta-N-acetylhexosaminidase
    Beta-hexosaminidase
    N-acetyl-beta-D-glucosaminidase
    N-acetyl-beta-glucosaminidase
    Gene namesi
    ORF Names:OG2516_04129Imported
    OrganismiOceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516)Imported
    Taxonomic identifieri314256 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeOceanicola
    Proteomesi
    • UP000003635 Componenti: Unassembled WGS sequence

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004309341 – 447Protein O-GlcNAcaseAdd BLAST447

    Interactioni

    Protein-protein interaction databases

    STRINGi314256.OG2516_04129.

    Structurei

    Secondary structure

    1447
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 7Combined sources6
    Beta strandi10 – 12Combined sources3
    Helixi16 – 28Combined sources13
    Beta strandi33 – 36Combined sources4
    Turni42 – 49Combined sources8
    Helixi54 – 68Combined sources15
    Turni69 – 71Combined sources3
    Beta strandi73 – 78Combined sources6
    Helixi89 – 104Combined sources16
    Beta strandi109 – 113Combined sources5
    Turni123 – 128Combined sources6
    Helixi132 – 146Combined sources15
    Turni147 – 149Combined sources3
    Beta strandi150 – 156Combined sources7
    Helixi162 – 165Combined sources4
    Helixi169 – 171Combined sources3
    Helixi173 – 181Combined sources9
    Beta strandi186 – 190Combined sources5
    Beta strandi193 – 196Combined sources4
    Helixi202 – 212Combined sources11
    Beta strandi217 – 220Combined sources4
    Helixi226 – 228Combined sources3
    Helixi242 – 247Combined sources6
    Beta strandi249 – 253Combined sources5
    Helixi259 – 262Combined sources4
    Helixi263 – 274Combined sources12
    Helixi280 – 291Combined sources12
    Helixi292 – 295Combined sources4
    Helixi306 – 315Combined sources10
    Helixi324 – 336Combined sources13
    Beta strandi338 – 341Combined sources4
    Helixi347 – 371Combined sources25
    Helixi376 – 404Combined sources29
    Helixi427 – 434Combined sources8
    Beta strandi435 – 437Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2XSAX-ray2.00A1-447[»]
    2XSBX-ray2.11A1-447[»]
    ProteinModelPortaliQ2CEE3.
    SMRiQ2CEE3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ2CEE3.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni219 – 221Substrate bindingImported3

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 84 family.Curated

    Phylogenomic databases

    eggNOGiENOG4105CPE. Bacteria.
    ENOG410XPBQ. LUCA.
    OrthoDBiPOG091H0IJT.

    Family and domain databases

    InterProiIPR011496. Beta-N-acetylglucosaminidase.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07555. NAGidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q2CEE3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLTGVIEGFY GRDWRRDERA TVMDWIAAAG MNTYIYGPKD DVHVRARWRV
    60 70 80 90 100
    PYDAAGLARL TELRDAAAAR GMVFYVSLAP CLDVTYSDPQ DRAALLARVD
    110 120 130 140 150
    QLARAGLRNL VLLFDDIPSV LPEADRHRFD SFAEAQADLS NMVLRHLRGA
    160 170 180 190 200
    GHVVFCPTEY CGRMAGGDPR GSAYLQRLGS TLDPAIDIFW TGPEIVSEEI
    210 220 230 240 250
    VAAHLAAVGE VLRRRPVIWD NFHANDYDIR RVFAGPLGGR SRDILPLVAG
    260 270 280 290 300
    WITNPNNEAE ANFPAIHTTG AYLADPDYAP ERAIAAAVAA WQPRFRLAFG
    310 320 330 340 350
    DGAVPSDLVA LLCDLFWQPF ALGPETTRIL SALRAALTVP RPDPSDPAWR
    360 370 380 390 400
    AALEDLRDLK RRINKLFTLM TEIENRDLFH TFHNYLWEAQ EEVGHLVAYC
    410 420 430 440
    DWLDEAPPPG AVFPATDRIH NFYRRGFGVA VQDILQRDRQ GRYHHGV
    Length:447
    Mass (Da):50,038
    Last modified:April 4, 2006 - v1
    Checksum:iB06BDD37C16C2F94
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAOT01000018 Genomic DNA. Translation: EAR51054.1.
    RefSeqiWP_007254354.1. NZ_CH724107.1.

    Genome annotation databases

    EnsemblBacteriaiEAR51054; EAR51054; OG2516_04129.
    PATRICi28498282. VBIOceGra115923_0282.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAOT01000018 Genomic DNA. Translation: EAR51054.1.
    RefSeqiWP_007254354.1. NZ_CH724107.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2XSAX-ray2.00A1-447[»]
    2XSBX-ray2.11A1-447[»]
    ProteinModelPortaliQ2CEE3.
    SMRiQ2CEE3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi314256.OG2516_04129.

    Protein family/group databases

    CAZyiGH84. Glycoside Hydrolase Family 84.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiEAR51054; EAR51054; OG2516_04129.
    PATRICi28498282. VBIOceGra115923_0282.

    Phylogenomic databases

    eggNOGiENOG4105CPE. Bacteria.
    ENOG410XPBQ. LUCA.
    OrthoDBiPOG091H0IJT.

    Miscellaneous databases

    EvolutionaryTraceiQ2CEE3.

    Family and domain databases

    InterProiIPR011496. Beta-N-acetylglucosaminidase.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07555. NAGidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiOGA_OCEGH
    AccessioniPrimary (citable) accession number: Q2CEE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 26, 2014
    Last sequence update: April 4, 2006
    Last modified: November 2, 2016
    This is version 35 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference 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.