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B1MBZ3 (BIOB_MYCA9) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 47. 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:MAB_2684c
OrganismMycobacterium abscessus (strain ATCC 19977 / DSM 44196) [Complete proteome] [HAMAP]
Taxonomic identifier561007 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus

Protein attributes

Sequence length342 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 – 342342Biotin synthase HAMAP-Rule MF_01694
PRO_0000381476

Sites

Metal binding781Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding821Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding851Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1211Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1541Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2131Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2831Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
B1MBZ3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 13A4077E77C352A6

FASTA34236,960
        10         20         30         40         50         60 
MTETAELTAA TDADVLAVAR EQVLEQGVGL TQEQVLRVLQ LPDDRLEELL ALAHEVRMRW 

        70         80         90        100        110        120 
CGPEVEVEGI ISLKTGGCPE DCHFCSQSGL FASPVRSAWL DIPSLVEAAK QTAKSGATEF 

       130        140        150        160        170        180 
CIVAAVRGPD ERLLAQVAAG IEAIRNEVDI QIACSLGMLT QEQVDRLSAM GVHRYNHNLE 

       190        200        210        220        230        240 
TAKSHFPNVV TTHSWEERWD TLKMVREAGM EVCCGGILGM GETLEQRAEF AANLAELEPD 

       250        260        270        280        290        300 
EVPLNFLNPR PGTPFGDLEV LPASDALRAV AAFRLALPRT MLRFAGGREI TLGDLGAKQG 

       310        320        330        340 
ILGGINAVIV GNYLTTLGRP AEADLELLDD LQMPIKALNS SL 

« Hide

References

[1]"Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
Genoscope
Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19977 / DSM 44196.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU458896 Genomic DNA. Translation: CAM62764.1.
RefSeqYP_001703418.1. NC_010397.1.

3D structure databases

ProteinModelPortalB1MBZ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561007.MAB_2684c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM62764; CAM62764; MAB_2684c.
GeneID5965193.
KEGGmab:MAB_2684c.
PATRIC17977102. VBIMycAbs55940_2728.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMADETQALC.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycMABS36809-WGS:GSQO-2698-MONOMER.
MABS561007:GJTG-2698-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_MYCA9
AccessionPrimary (citable) accession number: B1MBZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 47 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