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Q0I355 (BIOB_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:HS_1010
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length331 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 – 331331Biotin synthase HAMAP-Rule MF_01694
PRO_0000381418

Sites

Metal binding661Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1101Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1411Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2011Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2731Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I355 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 299A6FF3A1763BC5

FASTA33136,715
        10         20         30         40         50         60 
MTIITINIPS LTPHPCVEYW SVCKVEALFE TPFLELVYQA AQVHRKHFNP QTIQLSTLMS 

        70         80         90        100        110        120 
IKTGGCPEDC SYCPQSARYH TGVQNQQLLC VEEIVEKAKI AKSRGAGRFC MGAAWRGPKP 

       130        140        150        160        170        180 
KDIEKITEII KAVKDLGLET CGTFGLLQDG MAEELKEAGL DYYNHNIDTA PEHYKEIIGT 

       190        200        210        220        230        240 
RDFDDRLNTL GKVRKAGLKV CCGGIVGMNE TRKERAGLIA SLANLDPQPE SVPINQLVKV 

       250        260        270        280        290        300 
EGTPLADAQE LDWTEFVRTI AVARITMPKS YVRLSAGRQG MSEEMQAMCF MAGANSIFYG 

       310        320        330 
DKLLVTVNPE EDGDQLLMAK LDLKPETQEN K 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25285.1.
RefSeqYP_719221.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I355.
SMRQ0I355. Positions 19-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_1010.

Proteomic databases

PRIDEQ0I355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI25285; ABI25285; HS_1010.
GeneID4240503.
KEGGhso:HS_1010.
PATRIC20282045. VBIHaeSom53361_1059.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2299228.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-1044-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_HISS1
AccessionPrimary (citable) accession number: Q0I355
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 3, 2006
Last modified: February 19, 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