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Protein
Submitted name:

Glucooligosaccharide oxidase

Gene
N/A
Organism
Sarocladium strictum (Black bundle disease fungus) (Acremonium strictum)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421ZincCombined sources
Binding sitei54 – 541FADCombined sources
Metal bindingi61 – 611ZincCombined sources
Binding sitei131 – 1311FAD; via carbonyl oxygenCombined sources
Binding sitei169 – 1691FAD; via amide nitrogen and carbonyl oxygenCombined sources
Binding sitei220 – 2201FAD; via amide nitrogen and carbonyl oxygenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 967FADCombined sources
Nucleotide bindingi154 – 1552FADCombined sources
Nucleotide bindingi159 – 1635FADCombined sources
Nucleotide bindingi451 – 4533FADCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, Metal-bindingCombined sources, Nucleotide-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BRENDAi1.1.99.B3. 10953.

Names & Taxonomyi

Protein namesi
Submitted name:
Glucooligosaccharide oxidaseImported
OrganismiSarocladium strictum (Black bundle disease fungus) (Acremonium strictum)Imported
Taxonomic identifieri5046 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreales incertae sedisSarocladium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 499480Sequence analysisPRO_5004278602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 80Combined sources
Glycosylationi330 – 3301N-linked (GlcNAc...)Combined sourcesCAR_5005389964
Glycosylationi366 – 3661N-linked (GlcNAc...)Combined sourcesCAR_5005389963

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZR6X-ray1.55A26-499[»]
2AXRX-ray1.98A26-499[»]
3HSUX-ray1.69A26-499[»]
ProteinModelPortaliQ6PW77.
SMRiQ6PW77. Positions 26-499.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6PW77.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 230173FAD-binding PCMH-typeInterPro annotationAdd
BLAST

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR012951. BBE.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
PfamiPF08031. BBE. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PW77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRIQELTAA LSLASVVQAS WIQKRNSINA CLAAADVEFH EEDSEGWDMD
60 70 80 90 100
GTAFNLRVDY DPAAIAIPRS TEDIAAAVQC GLDAGVQISA KGGGHSYGSY
110 120 130 140 150
GFGGEDGHLM LELDRMYRVS VDDNNVATIQ GGARLGYTAL ELLDQGNRAL
160 170 180 190 200
SHGTCPAVGV GGHVLGGGYG FATHTHGLTL DWLIGATVVL ADASIVHVSE
210 220 230 240 250
TENADLFWAL RGGGGGFAIV SEFEFNTFEA PEIITTYQVT TTWNRKQHVA
260 270 280 290 300
GLKALQDWAQ NTMPRELSMR LEINANALNW EGNFFGNAKD LKKILQPIMK
310 320 330 340 350
KAGGKSTISK LVETDWYGQI NTYLYGADLN ITYNYDVHEY FYANSLTAPR
360 370 380 390 400
LSDEAIQAFV DYKFDNSSVR PGRGWWIQWD FHGGKNSALA AVSNDETAYA
410 420 430 440 450
HRDQLWLWQF YDSIYDYENN TSPYPESGFE FMQGFVATIE DTLPEDRKGK
460 470 480 490
YFNYADTTLT KEEAQKLYWR GNLEKLQAIK AKYDPEDVFG NVVSVEPIA
Length:499
Mass (Da):55,237
Last modified:July 5, 2004 - v1
Checksum:iBCB56CF1F4E922CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY573966 mRNA. Translation: AAS79317.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY573966 mRNA. Translation: AAS79317.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZR6X-ray1.55A26-499[»]
2AXRX-ray1.98A26-499[»]
3HSUX-ray1.69A26-499[»]
ProteinModelPortaliQ6PW77.
SMRiQ6PW77. Positions 26-499.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.1.99.B3. 10953.

Miscellaneous databases

EvolutionaryTraceiQ6PW77.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR012951. BBE.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR006094. Oxid_FAD_bind_N.
IPR006093. Oxy_OxRdtase_FAD_BS.
[Graphical view]
PfamiPF08031. BBE. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
PS00862. OX2_COVAL_FAD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Chen C.-T., Hsu E.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Structural characterization of glucooligosaccharide oxidase from Acremonium strictum."
    Lee M.H., Lai W.L., Lin S.F., Hsu C.S., Liaw S.H., Tsai Y.C.
    Appl. Environ. Microbiol. 71:8881-8887(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD."
    Huang C.H., Lai W.L., Lee M.H., Chen C.J., Vasella A., Tsai Y.C., Liaw S.H.
    J. Biol. Chem. 280:38831-38838(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 26-499 IN COMPLEX WITH FAD AND ZINC, DISULFIDE BONDS, GLYCOSYLATION AT ASN-330 AND ASN-366.
  4. "Functional roles of the 6-S-cysteinyl, 8alpha-N1-histidyl FAD in glucooligosaccharide oxidase from Acremonium strictum."
    Huang C.H., Winkler A., Chen C.L., Lai W.L., Tsai Y.C., Macheroux P., Liaw S.H.
    J. Biol. Chem. 283:30990-30996(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 26-499 IN COMPLEX WITH FAD AND ZINC, DISULFIDE BONDS, GLYCOSYLATION AT ASN-330 AND ASN-366.

Entry informationi

Entry nameiQ6PW77_SARSR
AccessioniPrimary (citable) accession number: Q6PW77
Entry historyi
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: March 16, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.