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Protein

Biotin synthase

Gene

bioB

Organism
Cupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424))
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 bindingi76 – 761Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi80 – 801Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi83 – 831Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi120 – 1201Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi151 – 1511Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi211 – 2111Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi283 – 2831Iron-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

BioCyciCTAI164546:GJNE-126-MONOMER.
CTAI977880:GLC7-126-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:RALTA_A0126
OrganismiCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424))
Taxonomic identifieri164546 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000001692 Componenti: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Biotin synthasePRO_0000381336Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi164546.RALTA_A0126.

Structurei

3D structure databases

ProteinModelPortaliB2AGA0.
SMRiB2AGA0. Positions 29-336.
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.

B2AGA0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQAHTVTTI SAESLRQTAR PHALPDDAKW RVDDVAALFA LPFNDLLFRA
60 70 80 90 100
QQVHREHFDA NTVQLSTLLS IKTGGCEEDC GYCPQSAHHD AGVKAEKLMA
110 120 130 140 150
LEEVLDAARA AKANGATRFC MGAAWRSPKD RHLEPVMDMV REVKAMGLET
160 170 180 190 200
CVTLGMLKAE QAQQLKEAGL DYYNHNLDTS PEFYGKIITT RTYQDRLDTI
210 220 230 240 250
GYVRDAGINV CCGGIVGMGE SREARAGLIA QLANMDPYPE SVPINNLVQV
260 270 280 290 300
EGTPLAGTEA LDPFEFVRTI AVARITMPRA MVRLSAGREA MDEALQALCF
310 320 330 340
MAGANSIFYG EKLLTTGNPQ ADRDRALLAR LDIRAEGYAG
Length:340
Mass (Da):37,164
Last modified:May 20, 2008 - v1
Checksum:iB376C88B8CF8FCF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633749 Genomic DNA. Translation: CAP62799.1.

Genome annotation databases

EnsemblBacteriaiCAP62799; CAP62799; RALTA_A0126.
KEGGicti:RALTA_A0126.
PATRICi21526882. VBICupTai42494_0127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU633749 Genomic DNA. Translation: CAP62799.1.

3D structure databases

ProteinModelPortaliB2AGA0.
SMRiB2AGA0. Positions 29-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi164546.RALTA_A0126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAP62799; CAP62799; RALTA_A0126.
KEGGicti:RALTA_A0126.
PATRICi21526882. VBICupTai42494_0127.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciCTAI164546:GJNE-126-MONOMER.
CTAI977880:GLC7-126-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: R1 / LMG 19424.

Entry informationi

Entry nameiBIOB_CUPTR
AccessioniPrimary (citable) accession number: B2AGA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 20, 2008
Last modified: April 29, 2015
This is version 51 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.