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B0SDC5 (BIOB_LEPBA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:LBF_0798
OrganismLeptospira biflexa serovar Patoc (strain Patoc 1 / Ames) [Complete proteome] [HAMAP]
Taxonomic identifier355278 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length351 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 – 351351Biotin synthase HAMAP-Rule MF_01694
PRO_0000381442

Sites

Metal binding641Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding681Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding711Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1081Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1401Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2001Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2691Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SDC5 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 04CFBD924BF2B1B6

FASTA35139,131
        10         20         30         40         50         60 
MIAEVQEKTI SSSPSIISEE EALQILKGEV PLLPVVAKAS EERFRHFGNR VRIHILDNIK 

        70         80         90        100        110        120 
NGYCPEDCGY CAQRKGGESG IQEYSLKSPE EIWEDAKKAK ENGAYRFCMV TSGRGPTDKA 

       130        140        150        160        170        180 
VDKLAETISK INGELGMKVC LSAGILDGKK AKTLKDAGLD RYNHNLNTSE SKYNEICSTH 

       190        200        210        220        230        240 
TFKDRLTTLE AAKEAEIGLC SGIIVGMGEE LKDIVQVAFE LKRLGVISIP VNFFIPIKGH 

       250        260        270        280        290        300 
AIQKSTLTPE FCVRVLSVFR LVNPDSEIRV GAGREGHLGF LQSMALYVAN SLFAEGYLNV 

       310        320        330        340        350 
KGSEMEQTMN LIRDCNMVPE FTEGIPEGWE DYDSKFLYDE KNFPELYKHK K 

« Hide

References

[1]"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis."
Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. expand/collapse author list , Davies J.K., Medigue C., Adler B.
PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Patoc 1 / Ames.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000777 Genomic DNA. Translation: ABZ93330.1.
RefSeqYP_001961908.1. NC_010842.1.

3D structure databases

ProteinModelPortalB0SDC5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING355278.LBF_0798.

Proteomic databases

PRIDEB0SDC5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ93330; ABZ93330; LBF_0798.
GeneID6390164.
KEGGlbf:LBF_0798.
PATRIC22340539. VBILepBif95142_0842.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMANCRFCAQ.
OrthoDBEOG622PMP.
ProtClustDBCLSK574240.

Enzyme and pathway databases

BioCycLBIF355278:GHTJ-797-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_LEPBA
AccessionPrimary (citable) accession number: B0SDC5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 43 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