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B2AGA0 (BIOB_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Biotin synthase

EC=2.8.1.6
Gene names
Name:bioB
Ordered Locus Names:RALTA_A0126
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length340 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 – 340340Biotin synthase HAMAP-Rule MF_01694
PRO_0000381336

Sites

Metal binding761Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding801Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding831Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1201Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1511Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2111Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2831Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B2AGA0 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: B376C88B8CF8FCF6

FASTA34037,164
        10         20         30         40         50         60 
MTQAHTVTTI SAESLRQTAR PHALPDDAKW RVDDVAALFA LPFNDLLFRA QQVHREHFDA 

        70         80         90        100        110        120 
NTVQLSTLLS IKTGGCEEDC GYCPQSAHHD AGVKAEKLMA LEEVLDAARA AKANGATRFC 

       130        140        150        160        170        180 
MGAAWRSPKD RHLEPVMDMV REVKAMGLET CVTLGMLKAE QAQQLKEAGL DYYNHNLDTS 

       190        200        210        220        230        240 
PEFYGKIITT RTYQDRLDTI GYVRDAGINV CCGGIVGMGE SREARAGLIA QLANMDPYPE 

       250        260        270        280        290        300 
SVPINNLVQV EGTPLAGTEA LDPFEFVRTI AVARITMPRA MVRLSAGREA MDEALQALCF 

       310        320        330        340 
MAGANSIFYG EKLLTTGNPQ ADRDRALLAR LDIRAEGYAG 

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU633749 Genomic DNA. Translation: CAP62799.1.
RefSeqYP_001795521.1. NC_010528.1.

3D structure databases

ProteinModelPortalB2AGA0.
SMRB2AGA0. Positions 29-336.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164546.RALTA_A0126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP62799; CAP62799; RALTA_A0126.
GeneID6301525.
KEGGcti:RALTA_A0126.
PATRIC21526882. VBICupTai42494_0127.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMADETQALC.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycCTAI164546:GJNE-126-MONOMER.
CTAI977880:GLC7-126-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_CUPTR
AccessionPrimary (citable) accession number: B2AGA0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 45 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