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Protein

Biotin synthase

Gene

bioB

Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196)
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 bindingi78 – 781Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi82 – 821Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi85 – 851Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi121 – 1211Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi154 – 1541Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi213 – 2131Iron-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

BioCyciMABS36809-WGS:GSQO-2698-MONOMER.
MABS561007:GJTG-2698-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:MAB_2684c
OrganismiMycobacterium abscessus (strain ATCC 19977 / DSM 44196)
Taxonomic identifieri561007 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium abscessus
ProteomesiUP000007137 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Biotin synthasePRO_0000381476Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi561007.MAB_2684c.

Structurei

3D structure databases

ProteinModelPortaliB1MBZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
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.

B1MBZ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTETAELTAA TDADVLAVAR EQVLEQGVGL TQEQVLRVLQ LPDDRLEELL
60 70 80 90 100
ALAHEVRMRW CGPEVEVEGI ISLKTGGCPE DCHFCSQSGL FASPVRSAWL
110 120 130 140 150
DIPSLVEAAK QTAKSGATEF CIVAAVRGPD ERLLAQVAAG IEAIRNEVDI
160 170 180 190 200
QIACSLGMLT QEQVDRLSAM GVHRYNHNLE TAKSHFPNVV TTHSWEERWD
210 220 230 240 250
TLKMVREAGM EVCCGGILGM GETLEQRAEF AANLAELEPD EVPLNFLNPR
260 270 280 290 300
PGTPFGDLEV LPASDALRAV AAFRLALPRT MLRFAGGREI TLGDLGAKQG
310 320 330 340
ILGGINAVIV GNYLTTLGRP AEADLELLDD LQMPIKALNS SL
Length:342
Mass (Da):36,960
Last modified:April 29, 2008 - v1
Checksum:i13A4077E77C352A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU458896 Genomic DNA. Translation: CAM62764.1.

Genome annotation databases

EnsemblBacteriaiCAM62764; CAM62764; MAB_2684c.
PATRICi17977102. VBIMycAbs55940_2728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU458896 Genomic DNA. Translation: CAM62764.1.

3D structure databases

ProteinModelPortaliB1MBZ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi561007.MAB_2684c.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAM62764; CAM62764; MAB_2684c.
PATRICi17977102. VBIMycAbs55940_2728.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
OMAiCAQSSHH.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.
BioCyciMABS36809-WGS:GSQO-2698-MONOMER.
MABS561007:GJTG-2698-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. "Acquisition of foreign virulence genes by the cystic fibrosis pathogen Mycobacterium abscessus."
    Genoscope
    Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L., Gaillard J.L.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19977 / DSM 44196.

Entry informationi

Entry nameiBIOB_MYCA9
AccessioniPrimary (citable) accession number: B1MBZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 29, 2008
Last modified: April 1, 2015
This is version 53 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.