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B2TL73

- BIOB_CLOBB

UniProt

B2TL73 - BIOB_CLOBB

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Protein

Biotin synthase

Gene

bioB

Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.UniRule annotation

Catalytic activityi

Dethiobiotin + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation
  • [2Fe-2S] clusterUniRule annotationNote: Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi69 – 691Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi106 – 1061Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi138 – 1381Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi198 – 1981Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi268 – 2681Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. biotin synthase activity Source: UniProtKB-HAMAP
  4. iron ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Biotin biosynthesis

Keywords - Ligandi

2Fe-2S, 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciCBOT508765:GJ4H-715-MONOMER.
UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
Ordered Locus Names:CLL_A0721
OrganismiClostridium botulinum (strain Eklund 17B / Type B)
Taxonomic identifieri935198 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001195: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Biotin synthasePRO_0000381312Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi508765.CLL_A0721.

Structurei

3D structure databases

ProteinModelPortaliB2TL73.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Biotin synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiFEIANEC.
OrthoDBiEOG622PMP.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB.
InterProiIPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view]
PfamiPF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF001619. Biotin_synth. 1 hit.
SMARTiSM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00433. bioB. 1 hit.

Sequencei

Sequence statusi: Complete.

B2TL73-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIVDKFKEK ILSGELISKK EAMILSKENI DELASAANDI RMSLCGKEFN
60 70 80 90 100
LCTIINGKSG RCGENCKYCA QSVYFKTDIE EYNLLDSESI ITSAISNYNN
110 120 130 140 150
GVHRFSVVTS GKKITNKEVH TVCKTYSELK DKCDIKLCAS HGLLNYEELV
160 170 180 190 200
KLKESGVIRY HNNLETSRNF FSNICTTHTF DEKTHTIKNA LKAGLQVCSG
210 220 230 240 250
GIIGLGETME DRIDMAFTLR ELNVDSIPIN ILNPIKGTAL ENQEKLSYDE
260 270 280 290 300
ITKTFALFRF ILPKKQIRLA GGRALLNDKG ERLMKSGVNA AISGDMLTTS
310
GIKTFDDIKM IKELGFEV
Length:318
Mass (Da):35,497
Last modified:July 1, 2008 - v1
Checksum:i0F47A586ECE2BC74
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001056 Genomic DNA. Translation: ACD21960.1.
RefSeqiWP_012422848.1. NC_010674.1.
YP_001884922.1. NC_010674.1.

Genome annotation databases

EnsemblBacteriaiACD21960; ACD21960; CLL_A0721.
GeneIDi19964803.
KEGGicbk:CLL_A0721.
PATRICi19394287. VBICloBot123574_0655.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001056 Genomic DNA. Translation: ACD21960.1 .
RefSeqi WP_012422848.1. NC_010674.1.
YP_001884922.1. NC_010674.1.

3D structure databases

ProteinModelPortali B2TL73.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 508765.CLL_A0721.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD21960 ; ACD21960 ; CLL_A0721 .
GeneIDi 19964803.
KEGGi cbk:CLL_A0721.
PATRICi 19394287. VBICloBot123574_0655.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239958.
KOi K01012.
OMAi FEIANEC.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci CBOT508765:GJ4H-715-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01694. BioB.
InterProi IPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view ]
Pfami PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF001619. Biotin_synth. 1 hit.
SMARTi SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00433. bioB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Clostridium botulinum strain Eklund."
    Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Eklund 17B / Type B.

Entry informationi

Entry nameiBIOB_CLOBB
AccessioniPrimary (citable) accession number: B2TL73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: November 26, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3