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Q7V6T8 (BIOB_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:PMT_1056
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

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_0000381545

Sites

Metal binding661Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding701Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1121Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1441Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2041Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2761Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V6T8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 91C9C4946EEA7C53

FASTA33536,889
        10         20         30         40         50         60 
MTVLIAKDLT FEPVVHRYDW TVDEVRELLE RPLMDLLWQA QLVHRTANPG YRVQLASLLS 

        70         80         90        100        110        120 
VKTGGCQEDC AYCPQSMHNS SDVEGQPDLV VQIQTVLERA RAAKDAGADR FCMGWAWREI 

       130        140        150        160        170        180 
RDGAQFEAML AMVSGVRELG LEACVTAGML TEKQASRLAD AGLTAYNHNL DTSPEYYDQI 

       190        200        210        220        230        240 
ITTRTYQERI ETLQKVRSAG ITLCCGGIIG MGESTVDRAS LLCVLANINP HPESVPINGL 

       250        260        270        280        290        300 
VAVEGTPLQD LPAVDPLEMV RMVATARILM PRSRVRLSAG REQLGREAQI LCLQAGADSI 

       310        320        330 
FYGDSLLTTS NPDVKTDREL LSQAGVHANW EESDE 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE21231.1.
RefSeqNP_894887.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V6T8.
SMRQ7V6T8. Positions 17-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT1056.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE21231; CAE21231; PMT_1056.
GeneID1727787.
KEGGpmt:PMT1056.
PATRIC23010475. VBIProMar135351_1387.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2391431.

Enzyme and pathway databases

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_PROMM
AccessionPrimary (citable) accession number: Q7V6T8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 1, 2003
Last modified: February 19, 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