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Q3SLY0 (BIOB_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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
Ordered Locus Names:Tbd_0319
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length317 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 – 317317Biotin synthase HAMAP-Rule MF_01694
PRO_0000381690

Sites

Metal binding571Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding611Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding641Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1011Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1321Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1921Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2641Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SLY0 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 94267387E863014F

FASTA31734,720
        10         20         30         40         50         60 
MNDMTPPVPR RSVSEIEALF ALPFADLMYQ AQGVHRAHFD PNRIQLSTLL SIKTGGCSED 

        70         80         90        100        110        120 
CGYCPQSVHY DAGVESQGLL DLGDVLKAAR AAKDAGASRF CMGAAWRGPK QRELEPVLAM 

       130        140        150        160        170        180 
VREVKALGLE TCATLGMLKD GQAEQLKEAG LDYYNHNLDT APEFYGEIIT TRDYQDRLDT 

       190        200        210        220        230        240 
LERVRRADLH VCCGGIVGMG ESRTQRAGLI AQLAALDPQP ESVPINLLVR VEGTPLAETE 

       250        260        270        280        290        300 
ALEPLEFVRT IAVTRLCMPK SFVRLSAGRQ QMSDAVQALC FLAGANSIFY GEKLLTTGNP 

       310 
EWERDQRLFD SLGVTAL 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ96272.1.
RefSeqYP_314077.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SLY0.
SMRQ3SLY0. Positions 9-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_0319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ96272; AAZ96272; Tbd_0319.
GeneID3672105.
KEGGtbd:Tbd_0319.
PATRIC23966779. VBIThiDen82923_0321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycTDEN292415:GHWG-322-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_THIDA
AccessionPrimary (citable) accession number: Q3SLY0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 11, 2005
Last modified: February 19, 2014
This is version 66 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