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Protein

Biotin synthase

Gene

bioB

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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

Pathway:ibiotin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes biotin from 7,8-diaminononanoate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. ATP-dependent dethiobiotin synthetase BioD (bioD)
  2. Biotin synthase (bioB)
This subpathway is part of the pathway biotin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes biotin from 7,8-diaminononanoate, the pathway biotin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi113 – 1131Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi205 – 2051Iron-sulfur 2 (2Fe-2S)UniRule annotation
Metal bindingi275 – 2751Iron-sulfur 2 (2Fe-2S)UniRule annotation

GO - Molecular functioni

GO - Biological processi

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

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:Cgl0072, cg0095
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
ProteomesiUP000000582 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Biotin synthasePRO_0000185551Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196627.cg0095.

Structurei

3D structure databases

ProteinModelPortaliP46396.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiKWCGPEV.
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.

P46396-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIPGTILDT ARTQVLEQGI GLNQQQLMEV LTLPEEQIPD LMELAHQVRL
60 70 80 90 100
KWCGEEIEVE GIISLKTGGC PEDCHFCSQS GLFESPVRSV WLDIPNLVEA
110 120 130 140 150
AKQTAKTGAT EFCIVAAVKG PDERLMTQLE EAVLAIHSEV EIEVAASIGT
160 170 180 190 200
LNKEQVDRLA AAGVHRYNHN LETARSYFPE VVTTHTWEER RETLRLVAEA
210 220 230 240 250
GMEVCSGGIL GMGETLEQRA EFAVQLAELD PHEVPMNFLD PRPGTPFADR
260 270 280 290 300
ELMDSRDALR SIGAFRLAMP HTMLRFAGGR ELTLGDKGSE QALLGGINAM
310 320 330
IVGNYLTTLG RPMEDDLDMM DRLQLPIKVL NKVI
Length:334
Mass (Da):36,856
Last modified:July 11, 2002 - v3
Checksum:iE0EF4E812C6BF096
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51G → A (PubMed:8173080).Curated
Sequence conflicti5 – 51G → A (PubMed:8917070).Curated
Sequence conflicti88 – 881R → A in BAA03169 (PubMed:8173080).Curated
Sequence conflicti113 – 1142CI → DF in BAA03169 (PubMed:8173080).Curated
Sequence conflicti232 – 2321H → D (PubMed:8173080).Curated
Sequence conflicti232 – 2321H → D (PubMed:8917070).Curated
Sequence conflicti260 – 2601R → A in BAA03169 (PubMed:8173080).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14084 Genomic DNA. Translation: BAA03169.1.
U31281 Genomic DNA. Translation: AAC44580.1.
BA000036 Genomic DNA. Translation: BAB97465.1.
BX927148 Genomic DNA. Translation: CAF18640.1.
PIRiI40338.
JC5084.
RefSeqiNP_599324.1. NC_003450.3.
WP_003861135.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB97465; BAB97465; BAB97465.
CAF18640; CAF18640; cg0095.
GeneIDi1021113.
KEGGicgb:cg0095.
cgl:NCgl0071.
PATRICi21492182. VBICorGlu203724_0073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14084 Genomic DNA. Translation: BAA03169.1.
U31281 Genomic DNA. Translation: AAC44580.1.
BA000036 Genomic DNA. Translation: BAB97465.1.
BX927148 Genomic DNA. Translation: CAF18640.1.
PIRiI40338.
JC5084.
RefSeqiNP_599324.1. NC_003450.3.
WP_003861135.1. NC_006958.1.

3D structure databases

ProteinModelPortaliP46396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg0095.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB97465; BAB97465; BAB97465.
CAF18640; CAF18640; cg0095.
GeneIDi1021113.
KEGGicgb:cg0095.
cgl:NCgl0071.
PATRICi21492182. VBICorGlu203724_0073.

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiKWCGPEV.
OrthoDBiEOG622PMP.

Enzyme and pathway databases

UniPathwayiUPA00078; UER00162.

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

« Hide 'large scale' publications
  1. "Analysis of the biotin biosynthesis pathway in coryneform bacteria: cloning and sequencing of the bioB gene from Brevibacterium flavum."
    Hatakeyama K., Kohama K., Vertes A.A., Kobayashi M., Kurusu Y., Yukawa H.
    DNA Seq. 4:87-93(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: MJ233.
  2. "Two new members of the bio B superfamily: cloning, sequencing and expression of bio B genes of Methylobacillus flagellatum and Corynebacterium glutamicum."
    Serebriiskii I.G., Vassin V.M., Tsygankov Y.D.
    Gene 175:15-22(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  3. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Entry informationi

Entry nameiBIOB_CORGL
AccessioniPrimary (citable) accession number: P46396
Secondary accession number(s): P94636
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 11, 2002
Last modified: July 22, 2015
This is version 118 of the entry and version 3 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.