SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P46396

- BIOB_CORGL

UniProt

P46396 - BIOB_CORGL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Biotin synthase
Gene
bioB, Cgl0072, cg0095
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
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 bindingi70 – 701Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi74 – 741Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi77 – 771Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal bindingi113 – 1131Iron-sulfur 2 (2Fe-2S) By similarity
Metal bindingi205 – 2051Iron-sulfur 2 (2Fe-2S) By similarity
Metal bindingi275 – 2751Iron-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

UniPathwayiUPA00078; UER00162.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin synthase (EC:2.8.1.6)
Gene namesi
Name:bioB
Ordered Locus Names:Cgl0072, cg0095
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000000582: Chromosome, UP000001009: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Biotin synthaseUniRule annotation
PRO_0000185551Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi196627.cg0095.

Structurei

3D structure databases

ProteinModelPortaliP46396.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0502.
HOGENOMiHOG000239958.
KOiK01012.
OMAiTCENTLR.
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

MTIPGTILDT ARTQVLEQGI GLNQQQLMEV LTLPEEQIPD LMELAHQVRL    50
KWCGEEIEVE GIISLKTGGC PEDCHFCSQS GLFESPVRSV WLDIPNLVEA 100
AKQTAKTGAT EFCIVAAVKG PDERLMTQLE EAVLAIHSEV EIEVAASIGT 150
LNKEQVDRLA AAGVHRYNHN LETARSYFPE VVTTHTWEER RETLRLVAEA 200
GMEVCSGGIL GMGETLEQRA EFAVQLAELD PHEVPMNFLD PRPGTPFADR 250
ELMDSRDALR SIGAFRLAMP HTMLRFAGGR ELTLGDKGSE QALLGGINAM 300
IVGNYLTTLG RPMEDDLDMM DRLQLPIKVL NKVI 334
Length:334
Mass (Da):36,856
Last modified:July 11, 2002 - v3
Checksum:iE0EF4E812C6BF096
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51G → A1 Publication
Sequence conflicti5 – 51G → A1 Publication
Sequence conflicti88 – 881R → A in BAA03169. 1 Publication
Sequence conflicti113 – 1142CI → DF in BAA03169. 1 Publication
Sequence conflicti232 – 2321H → D1 Publication
Sequence conflicti232 – 2321H → D1 Publication
Sequence conflicti260 – 2601R → A in BAA03169. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_224369.1. 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:
EMBL
GenBank
DDBJ
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 .
PIRi I40338.
JC5084.
RefSeqi NP_599324.1. NC_003450.3.
YP_224369.1. NC_006958.1.

3D structure databases

ProteinModelPortali P46396.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196627.cg0095.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB97465 ; BAB97465 ; BAB97465 .
CAF18640 ; CAF18640 ; cg0095 .
GeneIDi 1021113.
KEGGi cgb:cg0095.
cgl:NCgl0071.
PATRICi 21492182. VBICorGlu203724_0073.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00078 ; UER00162 .

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

« 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 9, 2014
This is version 108 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