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A0M7A9 (BIOB_GRAFK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:GFO_3566
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length363 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 – 363363Biotin synthase HAMAP-Rule MF_01694
PRO_0000381412

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 binding1291Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1891Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2611Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
A0M7A9 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: FC799A4D3A865CD4

FASTA36340,474
        10         20         30         40         50         60 
MALKHDWTKE EILEIYNKPF MELLYDAATI HREHHDPNTV QVSTLLSIKT GGCPEDCGYC 

        70         80         90        100        110        120 
PQAARYHTDL EGNDLMSVNQ VKAQALRAKA SGSSRVCMGA AWRNVKDGEE FDNVLEMVRS 

       130        140        150        160        170        180 
INKLDMEVCC TLGMLTENQA QRLAEAGLYA YNHNLDSSEE YYKEVISTRG YQDRLDTIGN 

       190        200        210        220        230        240 
VRKTNVTVCS GGIIGMGESE ADRAGMLVAL STLNPQPESV PINALVPVEG TPMEEQEPVP 

       250        260        270        280        290        300 
IWEMIRMVAT TRIVMPETQV RLSAGRTQMS REGQAMCFFA GANSIFAGDK LLTTPNPDVS 

       310        320        330        340        350        360 
EDMEMFKMLG LNPQKAFEKK SQPESVAAEK SKYQSQGEKP RWSRPEHKID RNLEAQQNAK 


TKA 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT0803.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU207366 Genomic DNA. Translation: CAL68504.1.
RefSeqYP_863571.1. NC_008571.1.

3D structure databases

ProteinModelPortalA0M7A9.
SMRA0M7A9. Positions 4-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING411154.GFO_3566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL68504; CAL68504; GFO_3566.
GeneID4651569.
KEGGgfo:GFO_3566.
PATRIC22075856. VBIGraFor5527_3438.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBCLSK2298548.

Enzyme and pathway databases

BioCycGFOR411154:GI79-3566-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_GRAFK
AccessionPrimary (citable) accession number: A0M7A9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: December 12, 2006
Last modified: February 19, 2014
This is version 54 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