Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Biotin synthase

Gene

bioB

Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
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), 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 bindingi53Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi57Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi60Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi97Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi128Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi188Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi260Iron-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:YE2907
OrganismiYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Taxonomic identifieri393305 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000000642 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003817191 – 350Biotin synthaseAdd BLAST350

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi393305.YE2907.

Structurei

3D structure databases

ProteinModelPortaliA1JS69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CZF. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239957.
KOiK01012.
OMAiPFDFIRM.
OrthoDBiPOG091H01DF.

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.

A1JS69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANYLRWTVG QAQALFEKPL LDLLFEAQQI HRQHFDPRQV QVSTLLSIKT
60 70 80 90 100
GACPEDCKYC PQSSRYKTGL ESERLMQVEQ VLESAKKAKA AGSTRFCMGA
110 120 130 140 150
AWKNPHERDM PYLEKMVEGV KAMGMETCMT LGTLDKQQAH RLADAGLDYY
160 170 180 190 200
NHNLDTSPEF YGSIITTRSY QERLDTLSEV RDAGIKVCSG GIVGLGETVR
210 220 230 240 250
DRAGLLVQLA NLPKPPESVP INMLVKVKGT PLENNDDVDA FEFIRTIAVA
260 270 280 290 300
RIMMPTSYVR LSAGREQMNE QTQAMCFMAG ANSIFYGCKL LTTPNPEEDK
310 320 330 340 350
DLQLFRKLGL NPQQTATQHG DRAQQQVLTE QLLHSDSLPE DSVQFYNAAH
Length:350
Mass (Da):39,199
Last modified:February 6, 2007 - v1
Checksum:i2EAA4E7F30B6C433
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286415 Genomic DNA. Translation: CAL12945.1.
RefSeqiWP_011816797.1. NC_008800.1.
YP_001007095.1. NC_008800.1.

Genome annotation databases

EnsemblBacteriaiCAL12945; CAL12945; YE2907.
GeneIDi4713711.
KEGGiyen:YE2907.
PATRICi18565475. VBIYerEnt11519_3091.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM286415 Genomic DNA. Translation: CAL12945.1.
RefSeqiWP_011816797.1. NC_008800.1.
YP_001007095.1. NC_008800.1.

3D structure databases

ProteinModelPortaliA1JS69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi393305.YE2907.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAL12945; CAL12945; YE2907.
GeneIDi4713711.
KEGGiyen:YE2907.
PATRICi18565475. VBIYerEnt11519_3091.

Phylogenomic databases

eggNOGiENOG4105CZF. Bacteria.
COG0502. LUCA.
HOGENOMiHOG000239957.
KOiK01012.
OMAiPFDFIRM.
OrthoDBiPOG091H01DF.

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_YERE8
AccessioniPrimary (citable) accession number: A1JS69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 6, 2007
Last modified: November 2, 2016
This is version 68 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.