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Q5N332 (BIOB_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:syc1098_d
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length320 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 – 320320Biotin synthase HAMAP-Rule MF_01694
PRO_0000381676

Sites

Metal binding541Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding581Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding611Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding981Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1301Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1901Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2621Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5N332 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: C2D5AD8892F576C2

FASTA32034,816
        10         20         30         40         50         60 
MEAIRHDWTL EEIEDLLNTP LLELVHRAQT VHRDYQPANA IQLATLLSVK TGGCSENCAY 

        70         80         90        100        110        120 
CPQSAHYNTE VDPQSTLPIE TVLEQAERAK AAGASRFCMG WAWREIRDGA QFDAMLEMVQ 

       130        140        150        160        170        180 
GVRQLGLEAC VTAGMLSDRQ AERLAEAGLT AYNHNLDTSP EFYGEIISTR TYADRLATLE 

       190        200        210        220        230        240 
RVRQAGISVC CGGIIGMGEG QRDRAGLLQV LATLNPHPES VPINALVPVE GTPLGDRDRL 

       250        260        270        280        290        300 
DPLDLVRMCA VARILMPKAR VRLSAGRTAL SREAQVLCFL AGANSIFYGD TLLTTANPVC 

       310        320 
EADRQLLADI GAEALEVVTA 

« Hide

References

[1]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008231 Genomic DNA. Translation: BAD79288.1.
RefSeqYP_171808.1. NC_006576.1.

3D structure databases

ProteinModelPortalQ5N332.
SMRQ5N332. Positions 5-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269084.syc1098_d.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD79288; BAD79288; syc1098_d.
GeneID3199271.
KEGGsyc:syc1098_d.
PATRIC32488024. VBISynElo117686_1271.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2297935.

Enzyme and pathway databases

BioCycSELO269084:GCDQ-1123-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_SYNP6
AccessionPrimary (citable) accession number: Q5N332
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 65 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