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Protein

Biotin synthase

Gene

bioB

Organism
Desulforudis audaxviator (strain MP104C)
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 bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi75 – 751Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi78 – 781Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi115 – 1151Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi147 – 1471Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi207 – 2071Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi277 – 2771Iron-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

BioCyciDAUD477974:GH0B-1360-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:Daud_1331
OrganismiDesulforudis audaxviator (strain MP104C)
Taxonomic identifieri477974 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeCandidatus Desulforudis
ProteomesiUP000008544: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Biotin synthasePRO_0000381345Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi477974.Daud_1331.

Structurei

3D structure databases

ProteinModelPortaliB1I4G4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
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.

B1I4G4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLQEKTAWI THVARRVIDG DTLSFEEATA LLQLPDAVTP FLLGWADVVR
60 70 80 90 100
KCFHGNRVDL CAIVNARAGR CSEDCRFCTQ AACYHTRAPV YPLLPAEGII
110 120 130 140 150
RRARAVRSQG IKRFSLVTSG RDPGGDFEKI LGITRQLKRE VPELKLCASL
160 170 180 190 200
GIISPTEARA LKEAGLDRYH HNLETAASFF PEVCTTHRYE DRVATIRAAQ
210 220 230 240 250
KVGLEVCAGG IIGLGEKPEQ RVELALALRE LGVTSVPVNI LHPVPGTPLA
260 270 280 290 300
TQPPLPALEI LRTLAVFRLL LPATTIRYAG GREHNLRDTQ VLGLAGGVDA
310 320
LITGDYLTTA GQGTARDRQL IRDLGLEG
Length:328
Mass (Da):35,720
Last modified:April 29, 2008 - v1
Checksum:i60847D68B5D104D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000860 Genomic DNA. Translation: ACA59841.1.
RefSeqiYP_001717473.1. NC_010424.1.

Genome annotation databases

EnsemblBacteriaiACA59841; ACA59841; Daud_1331.
GeneIDi6026707.
KEGGidau:Daud_1331.
PATRICi31969474. VBICanDes92303_1374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000860 Genomic DNA. Translation: ACA59841.1.
RefSeqiYP_001717473.1. NC_010424.1.

3D structure databases

ProteinModelPortaliB1I4G4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi477974.Daud_1331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA59841; ACA59841; Daud_1331.
GeneIDi6026707.
KEGGidau:Daud_1331.
PATRICi31969474. VBICanDes92303_1374.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciDAUD477974:GH0B-1360-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. "Complete sequence of chromosome of Desulforudis audaxviator MP104C."
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L., Hauser L., Kyrpides N., Ivanova N.N., Richardson P.
    Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MP104C.

Entry informationi

Entry nameiBIOB_DESAP
AccessioniPrimary (citable) accession number: B1I4G4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: March 4, 2015
This is version 45 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.