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Protein

Biotin synthase

Gene

bioB

Organism
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
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 bindingi51 – 511Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi95 – 951Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi126 – 1261Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi186 – 1861Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi258 – 2581Iron-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

BioCyciGOXY290633:GHB3-2029-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:GOX2031
OrganismiGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
Taxonomic identifieri290633 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter
ProteomesiUP000006375 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Biotin synthasePRO_0000381410Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290633.GOX2031.

Structurei

3D structure databases

ProteinModelPortaliQ5FPC9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
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.

Q5FPC9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRHDWTRDEV EALISLPFPE LMYRAQTLHR RYFDPTKVQI STLLSIKTGG
60 70 80 90 100
CPEDCAYCPQ SALHEKSVKA ERLMAVESVI KEARAAKKAG AGRFCMGAAW
110 120 130 140 150
RTPKDHDLDT VCEMIEGVKS LGLETCVTLG MLDAQQTERL KKAGLDYYNH
160 170 180 190 200
NLDTSEEFYG SIISTRTYQQ RLDTLSNVRD AGINVCCGGI VGMGEDLSDR
210 220 230 240 250
AGLLMTLANL PKHPESVPIN LLVRVEGTPL GEAEAVDPIT FVRIIATARI
260 270 280 290 300
MMPESHVRLA AGRENMTDEA HALCFLAGAN SIFCGEKLLT TPNPAEHRDR
310 320 330
QLLSALGMSP MVQSEAEMGT MRPAVTEDAV CEMAVS
Length:336
Mass (Da):36,889
Last modified:July 28, 2009 - v2
Checksum:i81873438FA3D40D1
GO

Sequence cautioni

The sequence AAW61767.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000009 Genomic DNA. Translation: AAW61767.1. Different initiation.

Genome annotation databases

EnsemblBacteriaiAAW61767; AAW61767; GOX2031.
KEGGigox:GOX2031.
PATRICi32611992. VBIGluOxy81109_2332.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000009 Genomic DNA. Translation: AAW61767.1. Different initiation.

3D structure databases

ProteinModelPortaliQ5FPC9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290633.GOX2031.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAW61767; AAW61767; GOX2031.
KEGGigox:GOX2031.
PATRICi32611992. VBIGluOxy81109_2332.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciGOXY290633:GHB3-2029-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. "Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
    Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
    Nat. Biotechnol. 23:195-200(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 621H.

Entry informationi

Entry nameiBIOB_GLUOX
AccessioniPrimary (citable) accession number: Q5FPC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 28, 2009
Last modified: July 22, 2015
This is version 73 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.