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Protein

Biotin synthase

Gene

bioB

Organism
Nitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
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: 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 bindingi68 – 681Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi72 – 721Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi75 – 751Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi112 – 1121Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi143 – 1431Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi203 – 2031Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi276 – 2761Iron-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

BioCyciNWIN323098:GJEG-247-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:Nwi_0243
OrganismiNitrobacter winogradskyi (strain Nb-255 / ATCC 25391)
Taxonomic identifieri323098 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
ProteomesiUP000002531 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Biotin synthasePRO_0000381507Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi323098.Nwi_0243.

Structurei

3D structure databases

ProteinModelPortaliQ3SW30.
SMRiQ3SW30. Positions 19-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiRIETLAC.
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.

Q3SW30-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSDPVSFDS SHDLMARPRH DWTRVEAETL YTTPFPDLLF QAQTIHRRHF
60 70 80 90 100
DPNHVETASL LSIKTGGCPE DCGYCAQSAH YDAGVKATKL MDKDAVLETA
110 120 130 140 150
RRAKDAGAGR FCMAAAWRHP KDRDLDRVCD MISAVKALGM ETCATLGMLT
160 170 180 190 200
PEQARRLQEA GLDFYNHNVD TSPEFYDKII TTRTMQDRIE TLACAREAGL
210 220 230 240 250
KLCCGGIIGM GEQVGDRLGM LILLANLDEH PESVPINLWN EVRGVPVNDT
260 270 280 290 300
ADRPDPIALV RMIAVARIMM PKSVVRLSAG RQYMTDELQA LCFVAGANSI
310 320 330 340
FIGDVLLTTK NPATLRDAAL LDRLGMSSPL DGVKMPAASP S
Length:341
Mass (Da):37,433
Last modified:October 11, 2005 - v1
Checksum:i224545513FF7C5C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000115 Genomic DNA. Translation: ABA03511.1.
RefSeqiWP_011313577.1. NC_007406.1.
YP_316863.1. NC_007406.1.

Genome annotation databases

EnsemblBacteriaiABA03511; ABA03511; Nwi_0243.
KEGGinwi:Nwi_0243.
PATRICi22696832. VBINitWin102302_0268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000115 Genomic DNA. Translation: ABA03511.1.
RefSeqiWP_011313577.1. NC_007406.1.
YP_316863.1. NC_007406.1.

3D structure databases

ProteinModelPortaliQ3SW30.
SMRiQ3SW30. Positions 19-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323098.Nwi_0243.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABA03511; ABA03511; Nwi_0243.
KEGGinwi:Nwi_0243.
PATRICi22696832. VBINitWin102302_0268.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiRIETLAC.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciNWIN323098:GJEG-247-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. "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
    Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
    Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Nb-255 / ATCC 25391.

Entry informationi

Entry nameiBIOB_NITWN
AccessioniPrimary (citable) accession number: Q3SW30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 11, 2005
Last modified: April 29, 2015
This is version 69 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

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.