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O67104 (BIOB_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. 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:aq_975
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length332 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 – 332332Biotin synthase HAMAP-Rule MF_01694
PRO_0000381206

Sites

Metal binding701Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding741Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding771Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1141Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1471Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2071Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2771Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
O67104 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 18C394EC7BC60B3F

FASTA33237,771
        10         20         30         40         50         60 
MDKVERRLYE LYEKAINYEP LSKEEALYIL EVDDIYVPFL VHLAQKIKKH YFPENEVEFC 

        70         80         90        100        110        120 
SIINAKSGAC SEDCKFCAQS KYYKTPINVY NLVPVDEMVE GAIRGVEFGA NRYCIVLSGK 

       130        140        150        160        170        180 
SATKEEVERI TEAVKEIKNE GLPINVCVSA GTLDEESLKK LKEAGVKRIN HNLETSRNFF 

       190        200        210        220        230        240 
KNIVTTHTWE DRYETIKRIK KVGLSTCSGG IFGMGESNED RVDMALTYRE LEVDSIPLNF 

       250        260        270        280        290        300 
LMPIEGTPME NAPGVEVMEA LKIIAMFRFT NPKAELRLCG GREQNLRDFH GMATLMTNAM 

       310        320        330 
MVGGYLTRAG RDIKKDYQLL KDLKAKRKVS VE 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07061.1.
PIRE70384.
RefSeqNP_213667.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67104.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_975.

Protocols and materials databases

DNASU1193738.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07061; AAC07061; aq_975.
GeneID1193738.
KEGGaae:aq_975.
PATRIC20959290. VBIAquAeo85532_0767.

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBCLSK2299571.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-700-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_AQUAE
AccessionPrimary (citable) accession number: O67104
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 89 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