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Protein

Biotin synthase

Gene

bioB

Organism
Streptococcus agalactiae serotype III (strain NEM316)
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. no protein annotated in this organism
  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 bindingi144Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi204Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi274Iron-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:gbs0511
OrganismiStreptococcus agalactiae serotype III (strain NEM316)
Taxonomic identifieri211110 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000823 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003816611 – 330Biotin synthaseAdd BLAST330

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi211110.gbs0511.

Structurei

3D structure databases

ProteinModelPortaliQ8E6Q1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CZF. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCGPCGGH.

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.

Q8E6Q1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFQTNYIHL ADEILSGKTS ISYEQALEIL NSDENWWEIY AAALYLKNQV
60 70 80 90 100
SRNNIRLNVL LSAKQGLCAE NCGYCSQSKE STADIDKFGL LPQNVILKQA
110 120 130 140 150
IVAHQNGASV FCIAMSGTKP SKREIEQLCQ VIPEIKKSLP LEICLTAGFL
160 170 180 190 200
DREQLHQLKQ AGIDRINHNL NTPEENYPNI ATTHSFKDRC DTLERIHNED
210 220 230 240 250
IDVCSGFICG MGESDEGLIT LAFRLKELNP YSIPVNFLLA VEGTPLGKYN
260 270 280 290 300
YLTPIKCLKI MAMLRFVFPF KELRLSAGRE VHFENFESLV TLLVDSTFLG
310 320 330
NYLTEGGRNQ HTDIEFLEKL QLNHTKKELI
Length:330
Mass (Da):37,337
Last modified:March 1, 2003 - v1
Checksum:iF47B4AC1B7DC6F29
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL766845 Genomic DNA. Translation: CAD46155.1.
RefSeqiWP_000009965.1. NC_004368.1.

Genome annotation databases

EnsemblBacteriaiCAD46155; CAD46155; CAD46155.
KEGGisan:gbs0511.
PATRICi19636868. VBIStrAga3577_0526.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL766845 Genomic DNA. Translation: CAD46155.1.
RefSeqiWP_000009965.1. NC_004368.1.

3D structure databases

ProteinModelPortaliQ8E6Q1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi211110.gbs0511.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAD46155; CAD46155; CAD46155.
KEGGisan:gbs0511.
PATRICi19636868. VBIStrAga3577_0526.

Phylogenomic databases

eggNOGiENOG4105CZF. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCGPCGGH.

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_STRA3
AccessioniPrimary (citable) accession number: Q8E6Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 81 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

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.