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Protein

Biotin synthase

Gene

bioB

Organism
Legionella pneumophila (strain Lens)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi61 – 611Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi98 – 981Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi129 – 1291Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi189 – 1891Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi261 – 2611Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
  2. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  3. biotin synthase activity Source: UniProtKB-HAMAP
  4. iron ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. biotin biosynthetic process Source: UniProtKB-HAMAP
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

BioCyciLPNE297245:GJD4-1677-MONOMER.
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:lpl1556
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517 Componenti: Chromosome

Organism-specific databases

LegioListilpl1556.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 315315Biotin synthasePRO_0000381441Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi297245.lpl1556.

Structurei

3D structure databases

ProteinModelPortaliQ5WW97.
SMRiQ5WW97. Positions 6-313.
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.

Q5WW97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEEKKQWSI SDIEAIYQQP FNDLLYQAHA IHRTYHDPNS LQFATLLSIK
60 70 80 90 100
TGACPEDCGY CSQSGHYKTH VEKEKLMSVE EVLQCAKEAK EGGAKRFCMG
110 120 130 140 150
AAWRCPPDKA IPQLKEMIEG VKSLGLETCM TLGMLTKEQA SHLKEAGLDY
160 170 180 190 200
YNHNIDTSPS YYDKVVTTRK FSDRLDTLNN VRSAGINVCC GGILGLGETR
210 220 230 240 250
EDRIEFLLTL ANMETPPESV PINRLIPVEG TPLAQAERVE GIELVRTIAT
260 270 280 290 300
ARILMPKSAI RLTAGRTEMS DELQALCYFA GANSVFIGDK LLTEDNPQRF
310
KDKTLFNKLG LTEMV
Length:315
Mass (Da):35,147
Last modified:November 22, 2004 - v1
Checksum:i40F4577393106BF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH15796.1.
RefSeqiYP_126902.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH15796; CAH15796; lpl1556.
KEGGilpf:lpl1556.
PATRICi22316807. VBILegPne33733_1730.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH15796.1.
RefSeqiYP_126902.1. NC_006369.1.

3D structure databases

ProteinModelPortaliQ5WW97.
SMRiQ5WW97. Positions 6-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi297245.lpl1556.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH15796; CAH15796; lpl1556.
KEGGilpf:lpl1556.
PATRICi22316807. VBILegPne33733_1730.

Organism-specific databases

LegioListilpl1556.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciLPNE297245:GJD4-1677-MONOMER.

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. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiBIOB_LEGPL
AccessioniPrimary (citable) accession number: Q5WW97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2009
Last sequence update: November 22, 2004
Last modified: March 31, 2015
This is version 82 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

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.