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P19206 (BIOB_LYSSH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. 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
OrganismLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifier1421 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

Protein attributes

Sequence length332 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 332332Biotin synthase HAMAP-Rule MF_01694
PRO_0000185545

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 binding2701Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P19206 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: B5FF14F5CA9903EF

FASTA33237,015
        10         20         30         40         50         60 
MNWLQLADEV IAGKVISDDE ALAILNSDDD DILKLMDGAF AIRKHYYGKK VKLNMIMNAK 

        70         80         90        100        110        120 
SGYCPEDCGY CSQSSKSTAP IEKYPFITKE EILAGAKRAF ENKIGTYCIV ASGRGPTRKD 

       130        140        150        160        170        180 
VNVVSEAVEE IKAKYGLKVC ACLGLLKEEQ AQQLKEAGVD RYNHNLNTSE RHHSYITTTH 

       190        200        210        220        230        240 
TYEDRVNTVE VVKKHGISPC SGAIIGMKET KMDVVEIARA LHQLDADSIP VNFLHAIDGT 

       250        260        270        280        290        300 
KLEGTQDLNP RYCLKVLALF RYMNPSKEIR ISGGREVNLG FLQPFGLYAA NSIFVGDYLT 

       310        320        330 
TEGQEANSDY RMLEDLGFEI ELTQKQEEAF CS 

« Hide

References

[1]"Cloning of the biotin synthetase gene from Bacillus sphaericus and expression in Escherichia coli and Bacilli."
Ohsawa I., Speck D., Kisou T., Hayakawa K., Zinsius M., Gloeckler R., Lemoine Y., Kamogawa K.
Gene 80:39-48(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: T-178-367.
[2]"Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin."
Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M., Villeval D., Kisou T., Kamogawa K., Lemoine Y.
Gene 87:63-70(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27867 Genomic DNA. Translation: AAA22268.1.
M29292 Genomic DNA. Translation: AAB02327.1.
PIRJS0274.

3D structure databases

ProteinModelPortalP19206.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_LYSSH
AccessionPrimary (citable) accession number: P19206
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 19, 2014
This is version 88 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