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Protein

Biotin synthase

Gene

bioB

Organism
Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
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 bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi78 – 781Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi81 – 811Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi117 – 1171Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi209 – 2091Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi279 – 2791Iron-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

BioCyciCURE504474:GJ8Y-466-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:cu0456
OrganismiCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
Taxonomic identifieri504474 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001727 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Biotin synthasePRO_0000381330Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi504474.cur_0456.

Structurei

3D structure databases

ProteinModelPortaliB1VF77.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
KOiK01012.
OMAiCAQSSHH.
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.

B1VF77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDISSQTPG ILATAREQVL QRGEGLSQEQ VLEVLNLPDE QIEELLALAH
60 70 80 90 100
EVRVKWCGEE VEIEGIVSLK TGGCPEDCHF CSQSGLFETP VRSVWLDIPL
110 120 130 140 150
LVEQAKQTAK TGATEFCIVA AVKGPDENLM RQLEVAVEAI RAEVDINVAA
160 170 180 190 200
SVGILTQEQV DRLTAIGVHR YNHNLETSRS NFPNVVTTHS WEERYETLKM
210 220 230 240 250
VKESGMEVCC GGILGMGETR EQRAEFAAEL ASLEPHEVPM NFLDPRPGTP
260 270 280 290 300
FADYPVMAGS EALKTIGAFR LALPRTTLRF AGGRELTLED FGTEAGLLGG
310 320 330
INGMIVGNYL TTLGRDQEAD VDMLNRLSLP IKALNRSV
Length:338
Mass (Da):36,989
Last modified:May 19, 2008 - v1
Checksum:iFC2EFE3D691EF66F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM942444 Genomic DNA. Translation: CAQ04416.1.
RefSeqiWP_012359709.1. NC_010545.1.
YP_001799850.1. NC_010545.1.

Genome annotation databases

EnsemblBacteriaiCAQ04416; CAQ04416; cu0456.
KEGGicur:cur_0456.
PATRICi21520628. VBICorUre58120_0457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM942444 Genomic DNA. Translation: CAQ04416.1.
RefSeqiWP_012359709.1. NC_010545.1.
YP_001799850.1. NC_010545.1.

3D structure databases

ProteinModelPortaliB1VF77.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi504474.cur_0456.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAQ04416; CAQ04416; cu0456.
KEGGicur:cur_0456.
PATRICi21520628. VBICorUre58120_0457.

Phylogenomic databases

eggNOGiCOG0502.
KOiK01012.
OMAiCAQSSHH.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciCURE504474:GJ8Y-466-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 lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
    Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
    J. Biotechnol. 136:11-21(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43042 / DSM 7109.

Entry informationi

Entry nameiBIOB_CORU7
AccessioniPrimary (citable) accession number: B1VF77
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 27, 2009
Last sequence update: May 19, 2008
Last modified: March 31, 2015
This is version 52 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.