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Protein

Biotin synthase

Gene

bioB

Organism
Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831)
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 = biotin + (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.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 bindingi67 – 671Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi112 – 1121Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi144 – 1441Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi204 – 2041Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi276 – 2761Iron-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

BioCyciMRAD426355:GJB5-5125-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:Mrad2831_5067
OrganismiMethylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831)
Taxonomic identifieri426355 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
ProteomesiUP000006589: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 337337Biotin synthasePRO_0000381470Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi426355.Mrad2831_5067.

Structurei

3D structure databases

ProteinModelPortaliB1LV19.
SMRiB1LV19. Positions 18-329.
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.

B1LV19-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSATSLPGSQ QPDLGEIRHD WSVAEIRAIH DLPLMDLVFR AAQVHRRHND
60 70 80 90 100
PADIQRASLL SIKTGGCPED CAYCPQSAHH KGAGVARERL MPVETVLAEA
110 120 130 140 150
AAAKAAGAQR FCMGAAWRQP KDGPEFDAVL AMVRGVRGLG MEACVTLGML
160 170 180 190 200
TPSQAGRLAE AGLTSYNHNL DTGPDFYEDI ISTRTYDERL QTLANVREAG
210 220 230 240 250
IGVCCGGIVG MGEGVTDRAA MLQVLANHAP HPESVPINAL VAVPGTPLED
260 270 280 290 300
QPAVDPFDLV RMCATARIVM PRSRVRLSAG RKSLTREAQV LCFLAGANSI
310 320 330
FYGERLLTTA NNGQDDDAAL LADLGIRVGE PVRAAAE
Length:337
Mass (Da):35,894
Last modified:April 29, 2008 - v1
Checksum:i0C3447DCF47CB229
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001001 Genomic DNA. Translation: ACB27025.1.
RefSeqiYP_001757708.1. NC_010505.1.

Genome annotation databases

EnsemblBacteriaiACB27025; ACB27025; Mrad2831_5067.
GeneIDi6141135.
KEGGimrd:Mrad2831_5067.
PATRICi22578556. VBIMetRad70578_5138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001001 Genomic DNA. Translation: ACB27025.1.
RefSeqiYP_001757708.1. NC_010505.1.

3D structure databases

ProteinModelPortaliB1LV19.
SMRiB1LV19. Positions 18-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi426355.Mrad2831_5067.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB27025; ACB27025; Mrad2831_5067.
GeneIDi6141135.
KEGGimrd:Mrad2831_5067.
PATRICi22578556. VBIMetRad70578_5138.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239957.
KOiK01012.
OMAiCGYCPQS.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciMRAD426355:GJB5-5125-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 Methylobacterium radiotolerans JCM 2831."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Mikhailova N., Marx C.J., Richardson P.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27329 / DSM 1819 / JCM 2831.

Entry informationi

Entry nameiBIOB_METRJ
AccessioniPrimary (citable) accession number: B1LV19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: January 7, 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.