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A1AWE7 (BIOB_RUTMC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:Rmag_0499
OrganismRuthia magnifica subsp. Calyptogena magnifica [Complete proteome] [HAMAP]
Taxonomic identifier413404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriasulfur-oxidizing symbionts

Protein attributes

Sequence length322 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 – 322322Biotin synthase HAMAP-Rule MF_01694
PRO_0000381591

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 binding1291Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1891Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2611Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AWE7 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 1C8E95F361741BC0

FASTA32236,131
        10         20         30         40         50         60 
MEELRNDWTL KEVEILFSLP FNDLLFQAHR IHRQNFDPNQ IQVSSLLNIK TGACPEDCSY 

        70         80         90        100        110        120 
CSQSSKYDTG LEREKLMEID LVLQQAKEAQ DIGATRFCMG AAWRNPTDKS LAKVILMIQG 

       130        140        150        160        170        180 
VKTMGMETCV TLGMLTQEQA FILKEAGLDY YNHNIDTSKE HYSNVVTTRN FQDRLNTLES 

       190        200        210        220        230        240 
VQNANIHVCS GGILGLDESQ TDRASMLRSL SNLRTHPDSV PFNLLVPIPG TPFENIEPPT 

       250        260        270        280        290        300 
ESEFVRTIAV ARIMMPKSVV RLSAGRTKMG EAMQALCFFA GANSIFYGEQ LLTTDNPNIN 

       310        320 
SDKDLFARLG INQKKVNNLQ SV 

« Hide

References

[1]"The Calyptogena magnifica chemoautotrophic symbiont genome."
Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J., Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M., Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.
Science 315:998-1000(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000488 Genomic DNA. Translation: ABL02254.1.
RefSeqYP_903725.1. NC_008610.1.

3D structure databases

ProteinModelPortalA1AWE7.
SMRA1AWE7. Positions 5-314.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING413404.Rmag_0499.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL02254; ABL02254; Rmag_0499.
GeneID4555123.
KEGGrma:Rmag_0499.
PATRIC32000675. VBICanRut45856_0556.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2320142.

Enzyme and pathway databases

BioCycCRUT413404:GHM7-519-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_RUTMC
AccessionPrimary (citable) accession number: A1AWE7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 52 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