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Q5PG48 (BIOB_SALPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. 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:SPA1958
OrganismSalmonella paratyphi A (strain ATCC 9150 / SARB42) [Complete proteome] [HAMAP]
Taxonomic identifier295319 [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_0000381603

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
Q5PG48 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 0AA49D48335B372D

FASTA34638,776
        10         20         30         40         50         60 
MARHPRWTLS QVTELFEKPL LELLFEAQQI HRQHFDPQQV QVSTLLSIKT GACPEDCKYC 

        70         80         90        100        110        120 
PQSSRYKTGL EAERLMEVEQ VLDSARKAKN AGSTRFCMGA AWKNPHERDM PYLEQIVQGV 

       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

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000026 Genomic DNA. Translation: AAV77867.1.
RefSeqYP_151179.1. NC_006511.1.

3D structure databases

ProteinModelPortalQ5PG48.
SMRQ5PG48. Positions 5-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING295319.SPA1958.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV77867; AAV77867; SPA1958.
PATRIC32353337. VBISalEnt134188_2092.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBPRK15108.

Enzyme and pathway databases

BioCycSENT295319:GJBZ-1958-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_SALPA
AccessionPrimary (citable) accession number: Q5PG48
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 67 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