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Protein

Biotin synthase

Gene

bioB

Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993))
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 bindingi54Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi58Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi61Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi98Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi129Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi189Iron-sulfur 2 (2Fe-2S)UniRule annotation1
Metal bindingi261Iron-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:Lferr_0436
OrganismiAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993))
Taxonomic identifieri380394 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAcidithiobacilliaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus
Proteomesi
  • UP000001856 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003811781 – 316Biotin synthaseAdd BLAST316

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi380394.Lferr_0436.

Structurei

3D structure databases

ProteinModelPortaliB5ELR8.
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.

B5ELR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNNSTALQTL DAILEIYARP FNDLIYAAQQ VHRLHFDPNA IQCSTLLSIK
60 70 80 90 100
TGGCPEDCGY CSQSVHHQTA LQAEPLMDLE QVRAAAREAK ANGAQRLCMG
110 120 130 140 150
AAWRSPHDRD IEKVAAMIGV VKEYGLESCV TLGMLKPGQA ERLQHAGLDY
160 170 180 190 200
YNHNLDTSPE FYGEVIHTRS YQDRLDTLEA VRDAGIRICS GGILGMGESR
210 220 230 240 250
RDRARMLQVL AQLPQAPESI PINALVPIPG TPLEAAEPID GFEFVRTVAV
260 270 280 290 300
TRILFPKAYV RLSAGREAMS DELQALAFLA GANSIFLGDR LLTTGNASTG
310
HDQALFNRLG LHRSAD
Length:316
Mass (Da):34,539
Last modified:October 14, 2008 - v1
Checksum:i1E0B22B466D83820
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001132 Genomic DNA. Translation: ACH82690.1.
RefSeqiWP_012536051.1. NC_011206.1.

Genome annotation databases

EnsemblBacteriaiACH82690; ACH82690; Lferr_0436.
KEGGiafe:Lferr_0436.
PATRICi20658394. VBIAciFer6930_0422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001132 Genomic DNA. Translation: ACH82690.1.
RefSeqiWP_012536051.1. NC_011206.1.

3D structure databases

ProteinModelPortaliB5ELR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi380394.Lferr_0436.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACH82690; ACH82690; Lferr_0436.
KEGGiafe:Lferr_0436.
PATRICi20658394. VBIAciFer6930_0422.

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_ACIF5
AccessioniPrimary (citable) accession number: B5ELR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 14, 2008
Last modified: November 2, 2016
This is version 54 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.