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Q826T2 (BIOB_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin synthase

EC=2.8.1.6
Gene names
Name:bioB
Synonyms:sav7093
Ordered Locus Names:SAV_7093
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism By similarity. HAMAP-Rule MF_01694

Catalytic activity

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_01694

Cofactor

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine By similarity.

Pathway

Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. HAMAP-Rule MF_01694

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01694

Sequence similarities

Belongs to the radical SAM superfamily. Biotin synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Biotin synthase HAMAP-Rule MF_01694
PRO_0000381663

Sites

Metal binding651Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding691Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding721Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1091Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1421Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2021Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2721Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q826T2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 4BF12B63B9D4EE74

FASTA38841,213
        10         20         30         40         50         60 
MDLLNTLVEK GLRRELPSRA EALAVLATSD DDVLDVVAAA GKVRRHWFGR RVKLNYLVNL 

        70         80         90        100        110        120 
KSGLCPEDCS YCSQRLGSKA EILKYTWLKP DEASQAAAAG LAGGAKRVCL VASGRGPTDR 

       130        140        150        160        170        180 
DVDRVSDTIK AIKDQNEGVE VCACLGLLSD GQADRLREAG ADAYNHNLNT SEGTYGDITT 

       190        200        210        220        230        240 
THTYADRVET VQKAHAAGLS ACSGLIAGMG ETDEDLVDVV YSLRELDPDS VPVNFLIPFE 

       250        260        270        280        290        300 
GTPLAKEWNL TPQRCLRILA MVRFVCPDVE VRIAGGREVH LRTMQPLALH LANSIFLGDY 

       310        320        330        340        350        360 
LTSEGQAGKA DLEMIADAGF EVEGADQVTL PEHRAPAGGC GSEQSAGCGS HEGGGACGSA 

       370        380 
PAPRTDEART DLVAVRRRGA GTDLAPNA 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000030 Genomic DNA. Translation: BAC74804.1.
RefSeqNP_828269.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ826T2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_7093.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC74804; BAC74804; SAV_7093.
GeneID1211657.
KEGGsma:SAV_7093.
PATRIC23728346. VBIStrAve112782_7512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMAWEERFIT.
OrthoDBEOG622PMP.
ProtClustDBPRK06256.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-7189-MONOMER.
UniPathwayUPA00078; UER00162.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01694. BioB.
InterProIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF001619. Biotin_synth. 1 hit.
SMARTSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00433. bioB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBIOB_STRAW
AccessionPrimary (citable) accession number: Q826T2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways