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Protein

Biotin synthase

Gene

bioB

Organism
Nocardioides sp. (strain BAA-499 / JS614)
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 bindingi66 – 661Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi110 – 1101Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi143 – 1431Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi203 – 2031Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi273 – 2731Iron-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

BioCyciNSP196162:GH4V-3462-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:Noca_3415
OrganismiNocardioides sp. (strain BAA-499 / JS614)
Taxonomic identifieri196162 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaeNocardioidaceaeNocardioides
ProteomesiUP000000640 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374Biotin synthasePRO_0000381509Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196162.Noca_3415.

Structurei

3D structure databases

ProteinModelPortaliA1SM80.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiYNINIQV.
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.

A1SM80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTSFDHLAD RILAGGDATP ADALAVLRAD EKDLLHVVAA AGRLRRARFG
60 70 80 90 100
NTVKVNYLVN LKSGLCPEDC HYCSQALGSR APILKYNWLS SEEVLEQAGA
110 120 130 140 150
GLRGGATRVC LVSSGRGPSD RDVDRVAAMA QELKGEQPGV EICACLGLLK
160 170 180 190 200
DGQAERLRAA GVDAYNHNIN TAESHHDTIV STHSYSDRVD TIEKAAAAGL
210 220 230 240 250
SPCSGLIAGL GETDEQLVEA LFALKALGAD SIPVNFLMPF DGTPSERTFE
260 270 280 290 300
LTPIRCVQIL AMTRFVCPDT EIRIAGGREM HLRSLQALAL HVANSIFLGD
310 320 330 340 350
YLTSEGQDAR ADLEMLRDNG FAILGAEAKP AGTATAAHRA QTAHDIAGGT
360 370
SVAGSAPDPA IRRRGAGTDV PANA
Length:374
Mass (Da):39,431
Last modified:February 6, 2007 - v1
Checksum:i657D95068D6F6A8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000509 Genomic DNA. Translation: ABL82915.1.
RefSeqiWP_011756849.1. NC_008699.1.
YP_924602.1. NC_008699.1.

Genome annotation databases

EnsemblBacteriaiABL82915; ABL82915; Noca_3415.
KEGGinca:Noca_3415.
PATRICi22748933. VBINocSp122728_3700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000509 Genomic DNA. Translation: ABL82915.1.
RefSeqiWP_011756849.1. NC_008699.1.
YP_924602.1. NC_008699.1.

3D structure databases

ProteinModelPortaliA1SM80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196162.Noca_3415.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL82915; ABL82915; Noca_3415.
KEGGinca:Noca_3415.
PATRICi22748933. VBINocSp122728_3700.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiYNINIQV.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciNSP196162:GH4V-3462-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 1 of Nocardioides sp. JS614."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., Richardson P.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BAA-499 / JS614.

Entry informationi

Entry nameiBIOB_NOCSJ
AccessioniPrimary (citable) accession number: A1SM80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 6, 2007
Last modified: April 1, 2015
This is version 59 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.