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A5IK57 (BIOB_THEP1) 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:Tpet_0559
OrganismThermotoga petrophila (strain RKU-1 / ATCC BAA-488 / DSM 13995) [Complete proteome] [HAMAP]
Taxonomic identifier390874 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length299 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 – 299299Biotin synthase HAMAP-Rule MF_01694
PRO_0000381685

Sites

Metal binding401Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding441Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding471Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1161Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1761Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2471Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A5IK57 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: A16B9D774A0ED6D0

FASTA29933,777
        10         20         30         40         50         60 
MKLKEILSME TKELILKANR MTSNLKLDLC SIVNAKSGIC DQDCKFCAQS SLYNTGVKKY 

        70         80         90        100        110        120 
PLLDKESILE KAKEAEKMGA IRFGIVTSGK RLTRKEILKV AKIIEFLKAN TNLKICASLG 

       130        140        150        160        170        180 
VLEKDELRYL KENGLDRYHH NLETSPGFFR NICTTHTFYD RVKTVENAKN VELEVCSGGI 

       190        200        210        220        230        240 
FGVGENFDDR LELAKILKDL EVDSVPINFL IPIRGTPFEN FQKLDVVERI RTIAMFRVVL 

       250        260        270        280        290 
GENVTIKIAA GREDFGDFQA LAFFAGANGM IVGGYLTLKG RSYDDDIKLI EGLRELMRW 

« Hide

References

[1]"Complete sequence of Thermotoga petrophila RKU-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RKU-1 / ATCC BAA-488 / DSM 13995.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000702 Genomic DNA. Translation: ABQ46580.1.
RefSeqYP_001244156.1. NC_009486.1.

3D structure databases

ProteinModelPortalA5IK57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING390874.Tpet_0559.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ46580; ABQ46580; Tpet_0559.
GeneID5170440.
KEGGtpt:Tpet_0559.
PATRIC23943878. VBIThePet65348_0565.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBCLSK2400226.

Enzyme and pathway databases

BioCycTPET390874:GHJI-574-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_THEP1
AccessionPrimary (citable) accession number: A5IK57
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 26, 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