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Q11S94 (BIOB_CYTH3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:CHU_2466
OrganismCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]
Taxonomic identifier269798 [NCBI]
Taxonomic lineageBacteriaBacteroidetesCytophagiaCytophagalesCytophagaceaeCytophaga

Protein attributes

Sequence length337 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 – 337337Biotin synthase HAMAP-Rule MF_01694
PRO_0000381341

Sites

Metal binding541Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding581Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding611Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding981Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1301Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1901Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2621Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11S94 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: D7B65D023605991D

FASTA33737,532
        10         20         30         40         50         60 
MTEIRNNWTK EEISAIYNSP ILDLMYRGAT VHREFHDPQE VQVCTLLSIK TGGCPEDCSY 

        70         80         90        100        110        120 
CPQAARYHTD VKVEKLMDVK DVLNSALEAK ESGSTRFCMG AAWREVRDNK DFDKVIDMVK 

       130        140        150        160        170        180 
GVSTMGMEVC CTLGMLTPEQ ADKLKDAGLY AYNHNLDTSA EHYDKVITTR TYDDRLETLD 

       190        200        210        220        230        240 
NVRNAKISVC SGGIIGMGES HGDRVGMLHT LANMVEHPES VPVNALVPVE GTPLEDQPRV 

       250        260        270        280        290        300 
SVWEMVRMIA TARIIMPKAM VRLSAGRVRM NTEEQALCFL AGANSIFAGD KLLTTPNPEV 

       310        320        330 
NADKEMFQVL NLKPRQSFKN GDAPKIKFEQ IPSALVK 

« Hide

References

[1]"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii."
Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J.
Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33406 / NCIMB 9469.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000383 Genomic DNA. Translation: ABG59720.1.
RefSeqYP_679062.1. NC_008255.1.

3D structure databases

ProteinModelPortalQ11S94.
SMRQ11S94. Positions 5-317.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269798.CHU_2466.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG59720; ABG59720; CHU_2466.
GeneID4184415.
KEGGchu:CHU_2466.
PATRIC21595811. VBICytHut34013_2464.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMARDFHGMA.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycCHUT269798:GJ83-2464-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_CYTH3
AccessionPrimary (citable) accession number: Q11S94
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 58 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