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Q7SID9 (Q7SID9_BREST) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein names
OrganismBrevibacterium sterolicum PDB 1I19
Taxonomic identifier1702 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeBrevibacteriaceaeBrevibacterium

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Contains FAD-binding PCMH-type domain. SAAS SAAS006094

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding64 – 718FAD PDB 1I19 PDB 2I0K
Nucleotide binding140 – 1434FAD PDB 1I19 PDB 2I0K

Sites

Active site2591Proton donor/acceptor PDB 1I19
Active site4231Proton donor/acceptor PDB 1I19
Binding site281FAD
Binding site1351FAD; via amide nitrogen PDB 1I19 PDB 2I0K
Binding site1501FAD PDB 1I19 PDB 2I0K
Binding site2061FAD; via carbonyl oxygen PDB 1I19 PDB 2I0K
Binding site2111FAD; via amide nitrogen and carbonyl oxygen PDB 1I19 PDB 2I0K
Binding site3801Cacodylate 1
Binding site4251Cacodylate 1
Binding site4251FAD PDB 1I19 PDB 2I0K
Binding site4901Cacodylate 2
Binding site5021Cacodylate 1
Binding site5271Cacodylate 2
Site4251Important for catalytic activity PDB 1I19

Sequences

Sequence LengthMass (Da)Tools
Q7SID9 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: D91FC2FD95D2102F

FASTA56161,519
        10         20         30         40         50         60 
STGPVAPLPT PPNFPNDIAL FQQAYQNWSK EIMLDATWVC SPKTPQDVVR LANWAHEHDY 

        70         80         90        100        110        120 
KIRPRGAMHG WTPLTVEKGA NVEKVILADT MTHLNGITVN TGGPVATVTA GAGASIEAIV 

       130        140        150        160        170        180 
TELQKHDLGW ANLPAPGVLS IGGALAVNAH GAALPAVGQT TLPGHTYGSL SNLVTELTAV 

       190        200        210        220        230        240 
VWNGTTYALE TYQRNDPRIT PLLTNLGRCF LTSVTMQAGP NFRQRCQSYT DIPWRELFAP 

       250        260        270        280        290        300 
KGADGRTFEK FVAESGGAEA IWYPFTEKPW MKVWTVSPTK PDSSNEVGSL GSAGSLVGKP 

       310        320        330        340        350        360 
PQAREVSGPY NYIFSDNLPE PITDMIGAIN AGNPGIAPLF GPAMYEITKL GLAATNANDI 

       370        380        390        400        410        420 
WGWSKDVQFY IKATTLRLTE GGGAVVTSRA NIATVINDFT EWFHERIEFY RAKGEFPLNG 

       430        440        450        460        470        480 
PVEIRCCGLD QAADVKVPSV GPPTISATRP RPDHPDWDVA IWLNVLGVPG TPGMFEFYRE 

       490        500        510        520        530        540 
MEQWMRSHYN NDDATFRPEW SKGWAFGPDP YTDNDIVTNK MRATYIEGVP TTENWDTARA 

       550        560 
RYNQIDPHRV FTNGFMDKLL P 

« Hide

References

[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 CACODYLATE AND FAD.

Cross-references

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I19X-ray1.70A/B1-561[»]
2I0KX-ray1.60A1-561[»]
ProteinModelPortalQ7SID9.
SMRQ7SID9. Positions 5-561.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProIPR015213. 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]
PfamPF09129. Chol_subst-bind. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7SID9.

Entry information

Entry nameQ7SID9_BREST
AccessionPrimary (citable) accession number: Q7SID9
Entry history
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: June 11, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)