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

Q5HDC9 (BIOB_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. 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:SACOL2426
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length335 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 – 335335Biotin synthase HAMAP-Rule MF_01694
PRO_0000381648

Sites

Metal binding611Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding651Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding681Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1041Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1371Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1971Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2671Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HDC9 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 0C7DAB4ECCB68A5B

FASTA33537,559
        10         20         30         40         50         60 
MNLAKRILQG EQLTKETVLK IYEDTNIDTL DLLNEAYILR KHYFGKKVKL NMILNAKSGI 

        70         80         90        100        110        120 
CPENCGYCGQ SRDIKQKQRY ALIPEEQIID GAKVAHDNHI GTYCIVMSGR GPSDKEVDHI 

       130        140        150        160        170        180 
SNTVRTIKSQ HPQLKICACL GLTNDEQAKK LKSAGVDRYN HNINTSENYH DNVVTTHSYK 

       190        200        210        220        230        240 
DRTDTIELMK ANNISPCSGV ICGMGESNQD IVDMAFALKE MDADSIPINF LHPIKGTKFG 

       250        260        270        280        290        300 
SMDDLTPMKC LRIVALFRLI NPTKEIRIAG GREVNLRSLQ PLALKAANSI FVGDYLITGG 

       310        320        330 
QPNQLDYDMI NDLGFEIDYD TCENKENKNE VSRAN 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: COL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW37250.1.
RefSeqYP_187228.1. NC_002951.2.

3D structure databases

ProteinModelPortalQ5HDC9.
SMRQ5HDC9. Positions 30-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93062.SACOL2426.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW37250; AAW37250; SACOL2426.
GeneID3238608.
KEGGsac:SACOL2426.
PATRIC19531131. VBIStaAur112458_2367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMARIMMPAS.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycSAUR93062:GCEP-2422-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_STAAC
AccessionPrimary (citable) accession number: Q5HDC9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 77 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