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Q5HSB2 (BIOB_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. 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:CJE1853
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length278 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 – 278278Biotin synthase HAMAP-Rule MF_01694
PRO_0000381288

Sites

Metal binding161Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding201Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding231Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding601Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding951Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1531Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HSB2 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 070B6A0D4F0599DC

FASTA27830,942
        10         20         30         40         50         60 
MQIMLCAISN IASGNCSEDC KYCTQSAHVK TDIQKYRRKE LSQIVLEAKM AKKNEALGFC 

        70         80         90        100        110        120 
LVTAGLGLDD EKLEYVCEAA KAVQKEAPNL LLIACNGMAS VEQLKELKKA GIFSYNHNLE 

       130        140        150        160        170        180 
SSKEFFPQIC TTHTWESRFQ TNLNAKEAGL MLCCGGIYGM GESEEDRLSF RKSLQELQPF 

       190        200        210        220        230        240 
STPINFFIAN ENLKLQVPRL SVDEALKIVR DTKEALPQSV VMVAGGREVV LRERQYEIFQ 

       250        260        270 
AGAGAIVIGD YLTTKGEEPS QDIIKLKEMG FTFASECH 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW36275.1.
RefSeqYP_179823.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HSB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE1853.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW36275; AAW36275; CJE1853.
GeneID3232480.
KEGGcjr:CJE1853.
PATRIC20045538. VBICamJej134361_1871.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMACATEDEA.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-1892-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_CAMJR
AccessionPrimary (citable) accession number: Q5HSB2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 66 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