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Protein

Biotin synthase

Gene

bioB

Organism
Synechococcus sp. (strain RCC307)
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 bindingi56 – 561Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi60 – 601Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi63 – 631Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi102 – 1021Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi134 – 1341Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi194 – 1941Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi266 – 2661Iron-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
Ordered Locus Names:SynRCC307_0793
OrganismiSynechococcus sp. (strain RCC307)
Taxonomic identifieri316278 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000001115 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 326326Biotin synthasePRO_0000381679Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi316278.SynRCC307_0793.

Structurei

3D structure databases

ProteinModelPortaliA5GS37.
SMRiA5GS37. Positions 6-317.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
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.

A5GS37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALIRHDWD LAEIEALLEL PLVDLLWHAQ QVHRDAHPAG YHVQLASLLS
60 70 80 90 100
VKTGGCEEDC AYCPQSMHHS SDVTAQPELQ LQVDGVLQQA RSARDAGAHR
110 120 130 140 150
FCMGWAWREI REGAPFDAML AMVRGVRELG MEACVTAGML TDSQAERLAQ
160 170 180 190 200
AGLTSYNHNL DTSPEHYDQI ISTRTYQERL DTLQRARDAG LSLCCGGIIG
210 220 230 240 250
MGESRRDRAS LLQVLAGLNP HPESVPINGL VAVEGTPLED QEPWEPLELV
260 270 280 290 300
RMVAVARILM PEARVRLSAG RERLSQEAQI LCLLAGADSI FYGDSLLTTS
310 320
NPAVQADQAL LAAAGVSSSL EGVAAA
Length:326
Mass (Da):35,348
Last modified:June 12, 2007 - v1
Checksum:i7E72DDC9ECB4464A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK27696.1.
RefSeqiWP_011935210.1. NC_009482.1.
YP_001227049.1. NC_009482.1.

Genome annotation databases

EnsemblBacteriaiCAK27696; CAK27696; SynRCC307_0793.
KEGGisyr:SynRCC307_0793.
PATRICi23822456. VBISynSp108374_0785.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT978603 Genomic DNA. Translation: CAK27696.1.
RefSeqiWP_011935210.1. NC_009482.1.
YP_001227049.1. NC_009482.1.

3D structure databases

ProteinModelPortaliA5GS37.
SMRiA5GS37. Positions 6-317.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316278.SynRCC307_0793.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAK27696; CAK27696; SynRCC307_0793.
KEGGisyr:SynRCC307_0793.
PATRICi23822456. VBISynSp108374_0785.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

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. Genoscope
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RCC307.

Entry informationi

Entry nameiBIOB_SYNR3
AccessioniPrimary (citable) accession number: A5GS37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 12, 2007
Last modified: April 29, 2015
This is version 56 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.