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B5YRL4 (BIOB_ECO5E) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:ECH74115_0923
OrganismEscherichia coli O157:H7 (strain EC4115 / EHEC) [Complete proteome] [HAMAP]
Taxonomic identifier444450 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_0000381360

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
B5YRL4 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 28BCA3F4E43B0EC5

FASTA34638,638
        10         20         30         40         50         60 
MAHRPRWTLS QVTELFEKPL LDLLFEAQQV HRQHFDPRQV QVSTLLSIKT GACPEDCKYC 

        70         80         90        100        110        120 
PQSSRYKTGL EAERLMEVEQ VLESARKAKA AGSTRFCMGA AWKNPHERDM SYLEQMVQGV 

       130        140        150        160        170        180 
KAMGLEACMT LGTLSESQAQ RLANAGLDYY NHNLDTSPEF YGNIITTRTY QERLDTLEKV 

       190        200        210        220        230        240 
RDAGIKVCSG GIVGLGETVK DRAGLLLQLA NLPTPPESVP INMLVKVKGT PLADNDDVDA 

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

       310        320        330        340 
DLQLFRKLGL NPQQTAVLAG DNEQQQRLEQ ALMTPDTDEY YNAAAL 

« Hide

References

[1]"Complete genome sequence of Escherichia coli O157:H7 str. EC4115."
Eppinger M., Sebastian Y., Ravel J.
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EC4115 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001164 Genomic DNA. Translation: ACI39836.1.
RefSeqYP_002269444.1. NC_011353.1.

3D structure databases

ProteinModelPortalB5YRL4.
SMRB5YRL4. Positions 3-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING444450.ECH74115_0923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACI39836; ACI39836; ECH74115_0923.
GeneID6967435.
KEGGecf:ECH74115_0923.
PATRIC18362642. VBIEscCol74651_1011.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
KOK01012.
OMAADRFCMG.
OrthoDBEOG622PMP.
ProtClustDBPRK15108.

Enzyme and pathway databases

BioCycECOL444450:GHOB-919-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_ECO5E
AccessionPrimary (citable) accession number: B5YRL4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 25, 2008
Last modified: February 19, 2014
This is version 43 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