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Protein

Biotin synthase

Gene

bioB

Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7)
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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi51 – 511Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi55 – 551Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi95 – 951Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi126 – 1261Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi186 – 1861Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi258 – 2581Iron-sulfur 2 (2Fe-2S)UniRule annotation

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

BioCyciBAPH561501:GHRN-286-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:BUAPTUC7_287
OrganismiBuchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7)
Taxonomic identifieri561501 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 343343Biotin synthasePRO_0000381257Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB8D7I5.
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.

B8D7I5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKWTLEET KMLFKKPFFN LMFQAQEEHR KNFDPNTIQI STLLSIKTGS
60 70 80 90 100
CPEDCKYCPQ SSRYKTGLKK EPLLEIEQIL SAAKKAKDSG SSRFCMGAAW
110 120 130 140 150
KNPKEKDMPY LEKIIKKIKE MGMETCMTLG TLNSTQAKKL ADAGLDFYNH
160 170 180 190 200
NLDTSKNFYS NIITTRTYQE RLHTLHAVRS SGMKVCSGGI IGLGEKKQDR
210 220 230 240 250
IELLMELSNL SIQPESVPIN MLVKIPGTPM ADNKDVEPFD FIRIIAVARI
260 270 280 290 300
MMPKSYIRLS AGRHKMNDQT QAMCFMAGAN SIFYGCKLLT SDNPEEKHDL
310 320 330 340
ELFKKLDLIP ENKTQTLLKE DEYKNIIKSS KIKKDQYYNA AII
Length:343
Mass (Da):39,198
Last modified:March 3, 2009 - v1
Checksum:i436F11FF78BEBAE8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001158 Genomic DNA. Translation: ACL30100.1.
RefSeqiWP_012619494.1. NC_011834.1.
YP_002468595.1. NC_011834.1.

Genome annotation databases

EnsemblBacteriaiACL30100; ACL30100; BUAPTUC7_287.
KEGGibau:BUAPTUC7_287.
PATRICi21248661. VBIBucAph26317_0285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001158 Genomic DNA. Translation: ACL30100.1.
RefSeqiWP_012619494.1. NC_011834.1.
YP_002468595.1. NC_011834.1.

3D structure databases

ProteinModelPortaliB8D7I5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACL30100; ACL30100; BUAPTUC7_287.
KEGGibau:BUAPTUC7_287.
PATRICi21248661. VBIBucAph26317_0285.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciBAPH561501:GHRN-286-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. "The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
    Moran N.A., McLaughlin H.J., Sorek R.
    Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Tuc7.

Entry informationi

Entry nameiBIOB_BUCAT
AccessioniPrimary (citable) accession number: B8D7I5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: June 24, 2015
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.