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P12678 (BIOB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. 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:STM0794
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length346 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 – 346346Biotin synthase HAMAP-Rule MF_01694
PRO_0000185561

Sites

Metal binding531Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding571Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding601Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding971Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1281Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1881Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2601Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P12678 [UniParc].

Last modified December 13, 2001. Version 2.
Checksum: A6C05B0C0F6BF42E

FASTA34638,804
        10         20         30         40         50         60 
MARHPRWTLS QVTELFEKPL LELLFEAQQI HRQHFDPQQV QVSTLLSIKT GACPEDCKYC 

        70         80         90        100        110        120 
PQSSRYKTGL EAERLMEVEQ VLDSARKAKN AGSTRFCMGA AWRNPHERDM PYLEKIVQGV 

       130        140        150        160        170        180 
KAMGLETCMT LGMLNESQAQ RLANAGLDYY NHNLDTSPEF YGNIITTRTY QERLDTLEKV 

       190        200        210        220        230        240 
REAGIKVCSG GIVGLGETVT DRAGLLLQLA NLPTPPESVP INMLVKVKGT PLADNDDVDA 

       250        260        270        280        290        300 
FDFIRTIAVA RIMMPTSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPAEDK 

       310        320        330        340 
DLQLFRKLGL NPQQTRVLAG DNEQQQRLEQ TLMTPDTDDY YNAAAL 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Transcriptional regulation and gene arrangement of Escherichia coli, Citrobacter freundii and Salmonella typhimurium biotin operons."
Shiuan D., Campbell A.
Gene 67:203-211(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL19731.1.
M21923 Genomic DNA. No translation available.
RefSeqNP_459772.1. NC_003197.1.

3D structure databases

ProteinModelPortalP12678.
SMRP12678. Positions 5-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM0794.

Proteomic databases

PRIDEP12678.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL19731; AAL19731; STM0794.
GeneID1252314.
KEGGstm:STM0794.
PATRIC32379961. VBISalEnt20916_0828.

Phylogenomic databases

HOGENOMHOG000239957.
KOK01012.
OMARIMMPAS.
OrthoDBEOG622PMP.
PhylomeDBP12678.

Enzyme and pathway databases

BioCycSENT99287:GCTI-799-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_SALTY
AccessionPrimary (citable) accession number: P12678
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: December 13, 2001
Last modified: July 9, 2014
This is version 118 of the entry and version 2 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