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A3M4U4 (BIOB_ACIBT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:A1S_1511
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length329 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 – 329329Biotin synthase HAMAP-Rule MF_01694
PRO_0000381172

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
A3M4U4 [UniParc].

Last modified September 2, 2008. Version 2.
Checksum: BB5D85217A783FF3

FASTA32936,659
        10         20         30         40         50         60 
MTLRNDWTRE EIQALYEQPF LDLVFKAQQV HREHFTANTI QVSTLLSIKT GKCPEDCKYC 

        70         80         90        100        110        120 
SQSAHYDSKL EAEKRIAVEK VISEAKAAKD SGSSRFCMGA AWRNPHERDM PYVLEMVREV 

       130        140        150        160        170        180 
KALGMETCMT LGMLNQSQAE RLKDAGLDYY NHNLDTSREY YSHIISTRTF DDRLNTLDYV 

       190        200        210        220        230        240 
RQAGMKVCSG GIVGLGESRE DRIGLLHELA TLPIHPESVP INMLVPIEGT PLADVEKLDV 

       250        260        270        280        290        300 
IEWIRTIAVA RIIMPHSYIR LSAGRESLSD SDQALAFMAG ANSLFSGDKL LTTPNAGEGK 

       310        320 
DQALFNKLGL TAEKPKPTVS DLSVDAMSA 

« Hide

References

[1]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17978 / NCDC KC 755.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000521 Genomic DNA. Translation: ABO11938.2.

3D structure databases

ProteinModelPortalA3M4U4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400667.A1S_1511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO11938; ABO11938; A1S_1511.
PATRIC20719266. VBIAciBau103176_1541.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239957.
OrthoDBEOG622PMP.
ProtClustDBCLSK2307451.

Enzyme and pathway databases

BioCycABAU400667:GI0Q-1499-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_ACIBT
AccessionPrimary (citable) accession number: A3M4U4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 2, 2008
Last modified: February 19, 2014
This is version 53 of the entry and version 2 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