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Q0BLD5 (BIOB_FRATO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:FTH_1245
OrganismFrancisella tularensis subsp. holarctica (strain OSU18) [Complete proteome] [HAMAP]
Taxonomic identifier393011 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length313 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 – 313313Biotin synthase HAMAP-Rule MF_01694
PRO_0000381396

Sites

Metal binding461Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding501Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding531Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding901Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1211Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1811Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2561Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BLD5 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 5135222D0015564C

FASTA31334,906
        10         20         30         40         50         60 
MTLQQIKEIY LRPLTELILK ALEIHNKNFG NDIELCSLKS IKTGTCPEDC KYCPQSGHYN 

        70         80         90        100        110        120 
TSIEKHKLLD KDSILAEAKN AKDAGSKRFC MGAAWKHIPK KDFDQVAEII TEVKNLGLET 

       130        140        150        160        170        180 
CVTLGSINAD EATKLKQAGL DYYNHNLDTS REFYPEIITT RKFEERIETI RNVANANINV 

       190        200        210        220        230        240 
CCGGILGMGE SLDDRFNLLL ELLQLPAAPK SIPINTLIPV KGTPLGDKYT NAQIDSFELV 

       250        260        270        280        290        300 
RFIATTRILF PQARLRLSAG RENMSLETQT LCFLAGINSI FYGNKLLTEN NATVNSDNFL 

       310 
LAKLGLKSNA ELC 

« Hide

References

[1]"Chromosome rearrangement and diversification of Francisella tularensis revealed by the type B (OSU18) genome sequence."
Petrosino J.F., Xiang Q., Karpathy S.E., Jiang H., Yerrapragada S., Liu Y., Gioia J., Hemphill L., Gonzalez A., Raghavan T.M., Uzman A., Fox G.E., Highlander S., Reichard M., Morton R.J., Clinkenbeard K.D., Weinstock G.M.
J. Bacteriol. 188:6977-6985(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OSU18.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000437 Genomic DNA. Translation: ABI83099.1.
RefSeqYP_763736.1. NC_008369.1.

3D structure databases

ProteinModelPortalQ0BLD5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393011.FTH_1245.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI83099; ABI83099; FTH_1245.
GeneID4307531.
KEGGfth:FTH_1245.
PATRIC17952563. VBIFraTul3936_1416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMARIMMPAS.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycFTUL393011:GHFN-1274-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_FRATO
AccessionPrimary (citable) accession number: Q0BLD5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 55 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