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Q97MI6 (BIOB_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 88. 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:CA_C0210
OrganismClostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) [Reference proteome] [HAMAP]
Taxonomic identifier272562 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length328 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 – 328328Biotin synthase HAMAP-Rule MF_01694
PRO_0000381308

Sites

Metal binding691Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding731Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding761Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding1121Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding1471Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2071Iron-sulfur 2 (2Fe-2S) By similarity
Metal binding2771Iron-sulfur 2 (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q97MI6 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 0C51144AB6D72C42

FASTA32836,428
        10         20         30         40         50         60 
MKNQWNNILS IGEKVLNGEK ITADEALTLS KSNGSDIFLL CSFANKLREK FNGNHVDLCS 

        70         80         90        100        110        120 
VINAKSGNCS EDCAFCAQSA HHKANVSCYP LLNEDKILEM AKQREAYGAR HCDIATSGLG 

       130        140        150        160        170        180 
YTGDEKDFQT ILKAFKKMKE NTNLKLCACL GTLTEKAMNS LAAVGVERYN HNLETAKSFY 

       190        200        210        220        230        240 
KNIVSTHGYD ERIKTINYAK NAKMEVCSGM IVGLGETMEQ RIEHALLLRD LNVDAVPVNI 

       250        260        270        280        290        300 
LNPVKGTKLE NAKPLSPMEI IKTFAIIRFI LPDKIIRYAG GREKNLRSLQ PLGFLSGLNG 

       310        320 
MLIGNYLTTN GQSVNDDFNM LKDLELEY 

« Hide

References

[1]"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum."
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.
J. Bacteriol. 183:4823-4838(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001437 Genomic DNA. Translation: AAK78192.1.
PIRE96925.
RefSeqNP_346852.1. NC_003030.1.

3D structure databases

ProteinModelPortalQ97MI6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272562.CA_C0210.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK78192; AAK78192; CA_C0210.
GeneID1116393.
KEGGcac:CA_C0210.
PATRIC32034715. VBICloAce74127_0395.

Phylogenomic databases

eggNOGCOG0502.
HOGENOMHOG000239958.
KOK01012.
OMATCENTLR.
OrthoDBEOG622PMP.

Enzyme and pathway databases

BioCycCACE272562:GJIH-232-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_CLOAB
AccessionPrimary (citable) accession number: Q97MI6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 88 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