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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)DescriptionActionsGraphical viewLength
Binding sitei28FADCombined sources1
Binding sitei135FAD; via amide nitrogenCombined sources1
Binding sitei150FADCombined sources1
Binding sitei206FAD; via carbonyl oxygenCombined sources1
Binding sitei211FAD; via amide nitrogen and carbonyl oxygenCombined sources1
Active sitei259Proton donor/acceptorCombined sources1
Active sitei423Proton donor/acceptorCombined sources1
Binding sitei425FADCombined sources1
Sitei425Important for catalytic activityCombined sources1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi64 – 71FADCombined sources8
Nucleotide bindingi140 – 143FADCombined sources4

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

FADCombined sourcesImported, Flavoprotein, Nucleotide-bindingCombined sourcesImported

Names & Taxonomyi

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

Pathology & Biotechi

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Structurei

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ7SID9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 221FAD-binding PCMH-typeInterPro annotationAdd BLAST191

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I19X-ray1.70A/B1-561[»]
2I0KX-ray1.60A1-561[»]
ProteinModelPortaliQ7SID9.
SMRiQ7SID9.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

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...

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: November 2, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sourcesImported

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.