Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Oxidoreductase

Gene
N/A
Organism
Brevibacterium sterolicum
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281FADCombined sources
Binding sitei135 – 1351FAD; via amide nitrogenCombined sources
Binding sitei150 – 1501FADCombined sources
Binding sitei206 – 2061FAD; via carbonyl oxygenCombined sources
Binding sitei211 – 2111FAD; via amide nitrogen and carbonyl oxygenCombined sources
Active sitei259 – 2591Proton donor/acceptorCombined sources
Active sitei423 – 4231Proton donor/acceptorCombined sources
Binding sitei425 – 4251FADCombined sources
Sitei425 – 4251Important for catalytic activityCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi64 – 718FADCombined sources
Nucleotide bindingi140 – 1434FADCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

FADCombined sources, Flavoprotein, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
OxidoreductaseImported
OrganismiBrevibacterium sterolicumImported
Taxonomic identifieri1702 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesBrevibacteriaceaeBrevibacterium

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I19X-ray1.70A/B1-561[»]
2I0KX-ray1.60A1-561[»]
ProteinModelPortaliQ7SID9.
SMRiQ7SID9. Positions 5-561.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SID9.

Family & Domainsi

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProiIPR015213. Cholesterol_OX_subst-bd.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR006094. Oxid_FAD_bind_N.
IPR016170. V_Alc_oxidase/Cytok_DH_C_dom.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF09129. Chol_subst-bind. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7SID9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
STGPVAPLPT PPNFPNDIAL FQQAYQNWSK EIMLDATWVC SPKTPQDVVR
60 70 80 90 100
LANWAHEHDY KIRPRGAMHG WTPLTVEKGA NVEKVILADT MTHLNGITVN
110 120 130 140 150
TGGPVATVTA GAGASIEAIV TELQKHDLGW ANLPAPGVLS IGGALAVNAH
160 170 180 190 200
GAALPAVGQT TLPGHTYGSL SNLVTELTAV VWNGTTYALE TYQRNDPRIT
210 220 230 240 250
PLLTNLGRCF LTSVTMQAGP NFRQRCQSYT DIPWRELFAP KGADGRTFEK
260 270 280 290 300
FVAESGGAEA IWYPFTEKPW MKVWTVSPTK PDSSNEVGSL GSAGSLVGKP
310 320 330 340 350
PQAREVSGPY NYIFSDNLPE PITDMIGAIN AGNPGIAPLF GPAMYEITKL
360 370 380 390 400
GLAATNANDI WGWSKDVQFY IKATTLRLTE GGGAVVTSRA NIATVINDFT
410 420 430 440 450
EWFHERIEFY RAKGEFPLNG PVEIRCCGLD QAADVKVPSV GPPTISATRP
460 470 480 490 500
RPDHPDWDVA IWLNVLGVPG TPGMFEFYRE MEQWMRSHYN NDDATFRPEW
510 520 530 540 550
SKGWAFGPDP YTDNDIVTNK MRATYIEGVP TTENWDTARA RYNQIDPHRV
560
FTNGFMDKLL P
Length:561
Mass (Da):61,519
Last modified:December 15, 2003 - v1
Checksum:iD91FC2FD95D2102F
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I19X-ray1.70A/B1-561[»]
2I0KX-ray1.60A1-561[»]
ProteinModelPortaliQ7SID9.
SMRiQ7SID9. Positions 5-561.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SID9.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProiIPR015213. Cholesterol_OX_subst-bd.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR006094. Oxid_FAD_bind_N.
IPR016170. V_Alc_oxidase/Cytok_DH_C_dom.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF09129. Chol_subst-bind. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Oxygen access to the active site of cholesterol oxidase through a narrow channel is gated by an Arg-Glu pair."
    Coulombe R., Yue K.Q., Ghisla S., Vrielink A.
    J. Biol. Chem. 276:30435-30441(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH FAD, ACTIVE SITE.
  2. "Structural and kinetic analyses of the H121A mutant of cholesterol oxidase."
    Lim L., Molla G., Guinn N., Ghisla S., Pollegioni L., Vrielink A.
    Biochem. J. 400:13-22(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH FAD.

Entry informationi

Entry nameiQ7SID9_BREST
AccessioniPrimary (citable) accession number: Q7SID9
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: June 24, 2015
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.