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Q9KC26 (BIOB_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. 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:BH1748
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length333 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 – 333333Biotin synthase HAMAP-Rule MF_01694
PRO_0000381229

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
Q9KC26 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: AE4971F33C546413

FASTA33336,814
        10         20         30         40         50         60 
MNWIQLAQEV IEGKRISENE ALAILNSPDD ELLLLLQGAF TIRQTYYGKK VKLNMIMNAK 

        70         80         90        100        110        120 
SGFCPENCGY CSQSSISKAP IDAYPMVNKE TILEGAKRAH ELNVGTYCIV ASGRGPTNRD 

       130        140        150        160        170        180 
IDHVTEAVRE IKDTYGLKIC ACLGILKPEQ AEQLKAAGVD RYNHNVNTSA RHHDQITTSH 

       190        200        210        220        230        240 
TYEDRVNTVE VVKHSGISPC SGVIVGMKET KEDVVDMAFQ LRELDADSIP VNFLHAIDGT 

       250        260        270        280        290        300 
PLQGVHELTP IYCLKVLSLF RYVCPTKEIR ISGGREVNLK SLQPLGLYAA NSIFIGDYLT 

       310        320        330 
TAGQEETADH QILKDLGFEV ESVEEMKASL QGQ 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB05467.1.
PIRD83868.
RefSeqNP_242614.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KC26.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH1748.

Protocols and materials databases

DNASU892640.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB05467; BAB05467; BAB05467.
GeneID892640.
KEGGbha:BH1748.
PATRIC18940624. VBIBacHal18977_1825.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMARIMMPAS.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-1832-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_BACHD
AccessionPrimary (citable) accession number: Q9KC26
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 87 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