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Protein

Biotin synthase

Gene

bioB

Organism
Lysinibacillus sphaericus (Bacillus sphaericus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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 + 2 reduced [2Fe-2S] ferredoxin = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.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

Pathway: biotin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes biotin from 7,8-diaminononanoate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. ATP-dependent dethiobiotin synthetase BioD (bioD)
  2. Biotin synthase (bioB)
This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes biotin from 7,8-diaminononanoate, the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi68 – 681Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi108 – 1081Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi140 – 1401Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi200 – 2001Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi270 – 2701Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

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

UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthaseUniRule annotation (EC:2.8.1.6UniRule annotation)
Gene namesi
Name:bioBUniRule annotation
OrganismiLysinibacillus sphaericus (Bacillus sphaericus)
Taxonomic identifieri1421 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 332332Biotin synthasePRO_0000185545Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi444177.Bsph_3466.

Structurei

3D structure databases

ProteinModelPortaliP19206.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

P19206-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNWLQLADEV IAGKVISDDE ALAILNSDDD DILKLMDGAF AIRKHYYGKK
60 70 80 90 100
VKLNMIMNAK SGYCPEDCGY CSQSSKSTAP IEKYPFITKE EILAGAKRAF
110 120 130 140 150
ENKIGTYCIV ASGRGPTRKD VNVVSEAVEE IKAKYGLKVC ACLGLLKEEQ
160 170 180 190 200
AQQLKEAGVD RYNHNLNTSE RHHSYITTTH TYEDRVNTVE VVKKHGISPC
210 220 230 240 250
SGAIIGMKET KMDVVEIARA LHQLDADSIP VNFLHAIDGT KLEGTQDLNP
260 270 280 290 300
RYCLKVLALF RYMNPSKEIR ISGGREVNLG FLQPFGLYAA NSIFVGDYLT
310 320 330
TEGQEANSDY RMLEDLGFEI ELTQKQEEAF CS
Length:332
Mass (Da):37,015
Last modified:November 1, 1990 - v1
Checksum:iB5FF14F5CA9903EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27867 Genomic DNA. Translation: AAA22268.1.
M29292 Genomic DNA. Translation: AAB02327.1.
PIRiJS0274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27867 Genomic DNA. Translation: AAA22268.1.
M29292 Genomic DNA. Translation: AAB02327.1.
PIRiJS0274.

3D structure databases

ProteinModelPortaliP19206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi444177.Bsph_3466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

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.
ProtoNetiSearch...

Publicationsi

  1. "Cloning of the biotin synthetase gene from Bacillus sphaericus and expression in Escherichia coli and Bacilli."
    Ohsawa I., Speck D., Kisou T., Hayakawa K., Zinsius M., Gloeckler R., Lemoine Y., Kamogawa K.
    Gene 80:39-48(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: T-178-367.
  2. "Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin."
    Gloeckler R., Ohsawa I., Speck D., Ledoux C., Bernard S., Zinsius M., Villeval D., Kisou T., Kamogawa K., Lemoine Y.
    Gene 87:63-70(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiBIOB_LYSSH
AccessioniPrimary (citable) accession number: P19206
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: June 24, 2015
This is version 92 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

Direct protein sequencing

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.