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Q8FUD1 (BIOB_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:CE0089
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length334 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 – 334334Biotin synthase HAMAP-Rule MF_01694
PRO_0000381327

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 binding1131Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2051Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2751Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FUD1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E392C8CD764B09F7

FASTA33436,548
        10         20         30         40         50         60 
MPNTTSILDT ARHQVLGDGI GLDQSQLIEI LNLPDEDIPA LMELAHQVRL KWCGEEIEVE 

        70         80         90        100        110        120 
GIISLKTGGC PEDCHFCSQS GLFESPVRSV WLDIEQLVEA AKQTAKSGAT EFCIVAAVKG 

       130        140        150        160        170        180 
PDDKLMNQLE EAVAAIQREV DIEVAASVGS LTPEQVTRLA RAGVHRYNHN LETARSFFPQ 

       190        200        210        220        230        240 
VVTTHTWEER RETLRLVAEA GMEVCSGGIL GMGETLEQRA EFAVQLAELN PTEVPINFLD 

       250        260        270        280        290        300 
PRPGTPFADR PLMESEDALR AIGAFRLAMP HTMIRFAGGR ELTLGAEGSE QGLLGGINAI 

       310        320        330 
IVGNYLTTLG RPMEDDLEMM DRLQLPLKVL NKVI 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC16899.1.
RefSeqNP_736699.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FUD1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE0089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC16899; BAC16899; BAC16899.
GeneID1031994.
KEGGcef:CE0089.
PATRIC21486362. VBICorEff9312_0135.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000239958.
KOK01012.
OMAETHHNID.
OrthoDBEOG622PMP.

Enzyme and pathway databases

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_COREF
AccessionPrimary (citable) accession number: Q8FUD1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 70 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