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Protein

Biotin synthase

Gene

bioB

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
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

Pathwayi: 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)DescriptionActionsGraphical viewLength
Metal bindingi68Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi72Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi75Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi112Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi143Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi203Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi276Iron-sulfur 2 (2Fe-2S)UniRule annotation1

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
Ordered Locus Names:blr2095
ORF Names:id897
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
Proteomesi
  • UP000002526 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003812441 – 331Biotin synthaseAdd BLAST331

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224911.blr2095.

Structurei

3D structure databases

ProteinModelPortaliQ9AMS7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CZF. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239957.
InParanoidiQ9AMS7.
KOiK01012.
OMAiICTTHSW.
OrthoDBiPOG091H01DF.
PhylomeDBiQ9AMS7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB. 1 hit.
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.

Q9AMS7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDAAVQVQRK KASNGAQVRN HWNVEEAKAL YDLPFADLML QAQRAHRKNF
60 70 80 90 100
DPNHVETASL LSIKTGGCPE DCGYCSQSAH YATGLKATRL MRCADVVATA
110 120 130 140 150
QRAKDAGATR FCMAAAWRTP KDRDLDSVCD MVNAVKGLGM ETCVTLGTLT
160 170 180 190 200
PKHAARLAEA GLDFYNHNVD TSPEFYSKII TTRSLQDRID TLAHVRDAGI
210 220 230 240 250
KICCGGIIGM GERVEDRLGM LVLLANLPNY PESVPINLWN KIEGVPVEDT
260 270 280 290 300
AEPPDPIALV RLLATARVMM PRSVVRLSAG RQYMTDELQA LCFLAGANSI
310 320 330
FVGDVLLTTN NPKVDRDADL LARLGITSGL A
Length:331
Mass (Da):36,011
Last modified:June 1, 2001 - v1
Checksum:iBE11557840FC5B3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322013 Genomic DNA. Translation: AAG61070.1.
BA000040 Genomic DNA. Translation: BAC47360.1.
RefSeqiNP_768735.1. NC_004463.1.
WP_011084890.1. NZ_CP011360.1.

Genome annotation databases

EnsemblBacteriaiBAC47360; BAC47360; BAC47360.
GeneIDi1055459.
KEGGibja:blr2095.
PATRICi21187534. VBIBraJap65052_2029.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322013 Genomic DNA. Translation: AAG61070.1.
BA000040 Genomic DNA. Translation: BAC47360.1.
RefSeqiNP_768735.1. NC_004463.1.
WP_011084890.1. NZ_CP011360.1.

3D structure databases

ProteinModelPortaliQ9AMS7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224911.blr2095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC47360; BAC47360; BAC47360.
GeneIDi1055459.
KEGGibja:blr2095.
PATRICi21187534. VBIBraJap65052_2029.

Phylogenomic databases

eggNOGiENOG4105CZF. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239957.
InParanoidiQ9AMS7.
KOiK01012.
OMAiICTTHSW.
OrthoDBiPOG091H01DF.
PhylomeDBiQ9AMS7.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01694. BioB. 1 hit.
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...

Entry informationi

Entry nameiBIOB_BRADU
AccessioniPrimary (citable) accession number: Q9AMS7
Secondary accession number(s): Q79UC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 99 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

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 one 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.