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A4J1M3

- BIOB_DESRM

UniProt

A4J1M3 - BIOB_DESRM

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Protein
Biotin synthase
Gene
bioB, Dred_0430
Organism
Desulfotomaculum reducens (strain MI-1)
Status
Reviewed - 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 By similarity.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

Binds 1 4Fe-4S cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Binds 1 2Fe-2S cluster. The cluster is coordinated with 3 cysteines and 1 arginine By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi67 – 671Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi139 – 1391Iron-sulfur 2 (2Fe-2S) By similarity
Metal bindingi199 – 1991Iron-sulfur 2 (2Fe-2S) By similarity
Metal bindingi269 – 2691Iron-sulfur 2 (2Fe-2S) By similarity

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

BioCyciDRED349161:GHP6-463-MONOMER.
UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthase (EC:2.8.1.6)
Gene namesi
Name:bioB
Ordered Locus Names:Dred_0430
OrganismiDesulfotomaculum reducens (strain MI-1)
Taxonomic identifieri349161 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum
ProteomesiUP000001556: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321Biotin synthaseUniRule annotation
PRO_0000381350Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi349161.Dred_0430.

Structurei

3D structure databases

ProteinModelPortaliA4J1M3.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiCKEDCIF.
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.

A4J1M3-1 [UniParc]FASTAAdd to Basket

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MFSEIQEKIH SGEGITFQEA AYLSKAENLD ILQILSMAAQ VTANFANKKI    50
DLCSIVNAKS GSCSEDCKFC AQSVYYATGC QTYPLLNSVA ILEAAKRVEE 100
KGIHRFALVT SGKNLSNRDF DEVIKIYQVL REKTSLQLCA SLGLLDTSRA 150
LQLKKAGVST YHHNLECAES FFKRICTTHT YQQRVATIKS AQSAGLKICS 200
GGIISLGETM LQRLELAYEL KALGVDSVPI NVLNPILGTP LAGQQIMSSQ 250
DIIKTICLFR LILPTISLRF GGGIKESLGE LRVLGFPAGI NAVIIGNFLT 300
TTGYQIDREL SVIRSMGLNI S 321
Length:321
Mass (Da):34,996
Last modified:May 1, 2007 - v1
Checksum:i610819034ACEEB3D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000612 Genomic DNA. Translation: ABO48976.1.
RefSeqiWP_011876814.1. NC_009253.1.
YP_001111801.1. NC_009253.1.

Genome annotation databases

EnsemblBacteriaiABO48976; ABO48976; Dred_0430.
GeneIDi4955407.
KEGGidrm:Dred_0430.
PATRICi21726707. VBIDesRed82656_0452.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000612 Genomic DNA. Translation: ABO48976.1 .
RefSeqi WP_011876814.1. NC_009253.1.
YP_001111801.1. NC_009253.1.

3D structure databases

ProteinModelPortali A4J1M3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349161.Dred_0430.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO48976 ; ABO48976 ; Dred_0430 .
GeneIDi 4955407.
KEGGi drm:Dred_0430.
PATRICi 21726707. VBIDesRed82656_0452.

Phylogenomic databases

eggNOGi COG0502.
HOGENOMi HOG000239958.
KOi K01012.
OMAi CKEDCIF.
OrthoDBi EOG622PMP.

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .
BioCyci DRED349161:GHP6-463-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01694. BioB.
InterProi IPR013785. Aldolase_TIM.
IPR010722. BATS_dom.
IPR002684. Biotin_synth/BioAB.
IPR024177. Biotin_synthase.
IPR006638. Elp3/MiaB/NifB.
IPR007197. rSAM.
[Graphical view ]
Pfami PF06968. BATS. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF001619. Biotin_synth. 1 hit.
SMARTi SM00876. BATS. 1 hit.
SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00433. bioB. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MI-1.

Entry informationi

Entry nameiBIOB_DESRM
AccessioniPrimary (citable) accession number: A4J1M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 1, 2007
Last modified: September 3, 2014
This is version 50 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

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