Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B6J725 (BIOB_COXB1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:CbuK_0835
OrganismCoxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)) [Complete proteome] [HAMAP]
Taxonomic identifier434924 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length321 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 – 321321Biotin synthase HAMAP-Rule MF_01694
PRO_0000381331

Sites

Metal binding521Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding561Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding591Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding961Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1271Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1871Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2591Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J725 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: FDC79146CEC713D8

FASTA32136,252
        10         20         30         40         50         60 
MKGRNWNQAS VAKLFELPFF ELLYKAYETH RSHFDVRDME LCTLSSIKTG TCPEDCAYCP 

        70         80         90        100        110        120 
QSGHYKTDVE REKLINLEAV LEQAKVAKEN GARRFCMGAA WRSPPKRELP KVLEMIKSVK 

       130        140        150        160        170        180 
ALGLETCVTL GMLDQEQALQ LKEAGLDFYN HNLDTSPEFY KKIITTRTYQ DRMETLKNVR 

       190        200        210        220        230        240 
NAGINVCCGG ILGMGESRAD RIQLLLELYQ LPEPPTSIPI NQLIPIKGTP LENTKAIDPF 

       250        260        270        280        290        300 
EFIKTIAITR LLFPTSVIRL SAGREAMSDE LQAWCFMAGA NSIFYGDKLL TAKNPGQNRD 

       310        320 
VNLLKKLGLK VPVLTEEYAC Y 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuK_Q154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001020 Genomic DNA. Translation: ACJ20074.1.
RefSeqYP_002305219.1. NC_011528.1.

3D structure databases

ProteinModelPortalB6J725.
SMRB6J725. Positions 4-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434924.CbuK_0835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ20074; ACJ20074; CbuK_0835.
GeneID7015348.
KEGGcbc:CbuK_0835.
PATRIC17917091. VBICoxBur77120_0849.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycCBUR434924:GHWU-833-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_COXB1
AccessionPrimary (citable) accession number: B6J725
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 38 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