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Protein

Biotin synthase

Gene

bioB

Organism
Sulfurovum sp. (strain NBC37-1)
Status
Reviewed-Annotation score: 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 + 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:ibiotin 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 bindingi20 – 201Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi24 – 241Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi27 – 271Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi64 – 641Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi99 – 991Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi157 – 1571Iron-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

BioCyciSSP387093:GH25-91-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:SUN_0087
OrganismiSulfurovum sp. (strain NBC37-1)
Taxonomic identifieri387093 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaSulfurovum
ProteomesiUP000006378 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Biotin synthasePRO_0000381669Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi387093.SUN_0087.

Structurei

3D structure databases

ProteinModelPortaliA6Q6D8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
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.

A6Q6D8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTRKQIFLC AINNILSGTC KEDCKFCTQS VRYHADIERY SYKKIGQIVE
60 70 80 90 100
EARQAKANGA LGYCLVTAGK GLDDKKVDFV ARAAQAVKAE VEGLNLIACN
110 120 130 140 150
GTASLEQLIY LKEHGIDSYN HNLETSERYY PEICLTHGWQ ERYETCENVK
160 170 180 190 200
SSGLALCSGG IFGMGESMKD REDLLSAIAS LQPESTPLNF YHPNPALPIK
210 220 230 240 250
TRNIGFEEAL NIIRRAHTLL GEDRLLMVAG GRELLFNGKE DEMFKAGANS
260 270 280
IVIGDYLTTS GSAPKMDQLM LEKLGYEVAT SCDSH
Length:285
Mass (Da):31,480
Last modified:July 28, 2009 - v2
Checksum:i75AE4CB0EC3DEE76
GO

Sequence cautioni

The sequence BAF71047.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009179 Genomic DNA. Translation: BAF71047.1. Different initiation.
RefSeqiWP_041672621.1. NC_009663.1.

Genome annotation databases

EnsemblBacteriaiBAF71047; BAF71047; SUN_0087.
KEGGisun:SUN_0087.
PATRICi23773101. VBISulSp49917_0088.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009179 Genomic DNA. Translation: BAF71047.1. Different initiation.
RefSeqiWP_041672621.1. NC_009663.1.

3D structure databases

ProteinModelPortaliA6Q6D8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi387093.SUN_0087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF71047; BAF71047; SUN_0087.
KEGGisun:SUN_0087.
PATRICi23773101. VBISulSp49917_0088.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciSSP387093:GH25-91-MONOMER.

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. "Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
    Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
    Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NBC37-1.

Entry informationi

Entry nameiBIOB_SULNB
AccessioniPrimary (citable) accession number: A6Q6D8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 28, 2009
Last modified: July 22, 2015
This is version 58 of the entry and version 2 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

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.