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A0PP05 (BIOB_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:MUL_1563
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length350 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 – 350350Biotin synthase HAMAP-Rule MF_01694
PRO_0000381488

Sites

Metal binding861Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding901Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding931Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1291Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1621Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2211Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2911Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PP05 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 27E01439AE2971D5

FASTA35037,726
        10         20         30         40         50         60 
MVTQAATRPS NDAGQDGVTE PDILAVARQQ VLERGEGLNQ EQVLQVLQLS EDRLEELLVL 

        70         80         90        100        110        120 
AHDVRMRWCG PEVEVEGIIS LKTGGCPEDC HFCSQSGLFS SPVRSAWLDI PSLVEAAKQT 

       130        140        150        160        170        180 
AKSGATEFCI VAAVRGPDAR LLSQVAAGIE AIRNEVEINV ACSLGMLTAE QVEQLAAMGV 

       190        200        210        220        230        240 
HRYNHNLETA RSYFTNVVTT HTWEERWQTL TMVRDAGMEV CCGGILGMGE TLEQRAEFAA 

       250        260        270        280        290        300 
NLAELDPDEV PLNFLNPRPG TPFGDLEVLP AGEALKAVGA FRLALPRTML RFAGGREITL 

       310        320        330        340        350 
GDLGAKRGIL GGINAVIVGN YLTTLGRPAE ADLELLEDLQ MPLKALNASL 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL04074.1.
RefSeqYP_905545.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PP05.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_1563.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL04074; ABL04074; MUL_1563.
GeneID4552336.
KEGGmul:MUL_1563.
PATRIC18170039. VBIMycUlc37413_1874.

Organism-specific databases

GenoListMUL_1563.
CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBPRK06256.

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_MYCUA
AccessionPrimary (citable) accession number: A0PP05
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 54 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