Skip Header

Contribute Send feedback
Read comments (?) or add your own

B5EUP7 (BIOD_VIBFM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent dethiobiotin synthetase BioD
EC=6.3.3.3
Alternative name(s):
DTB synthetase
Short name=DTBS
Dethiobiotin synthase
Gene names
Name:bioD
Ordered Locus Names:VFMJ11_A0867
OrganismVibrio fischeri (strain MJ11) [Complete proteome] [HAMAP]
Taxonomic identifier388396 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Aliivibrio

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring By similarity. HAMAP MF_00336

Catalytic activity

ATP + 7,8-diaminononanoate + CO2 = ADP + phosphate + dethiobiotin. HAMAP MF_00336

Cofactor

Magnesium By similarity. HAMAP MF_00336

Pathway

Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. HAMAP MF_00336

Subcellular location

Cytoplasm By similarity HAMAP MF_00336.

Sequence similarities

Belongs to the dethiobiotin synthetase family.

Ontologies

Keywords
   Biological processBiotin biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processbiotin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

dethiobiotin synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 226226ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_1000119886

Regions

Nucleotide binding13 – 186ATP By similarity
Nucleotide binding116 – 1194ATP By similarity
Nucleotide binding176 – 1772ATP By similarity

Sites

Metal binding131Magnesium 1 By similarity
Metal binding171Magnesium 2 By similarity
Metal binding551Magnesium 2 By similarity
Metal binding1161Magnesium 2 By similarity
Binding site551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B5EUP7 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 43B797D856C363C1

FASTA22624,409
        10         20         30         40         50         60 
MIDAFFIAGT DTDVGKTVAS KAILDALNMK GLRTAAYKPV AAGSEDKGEG VQNSDAIHLR 

        70         80         90        100        110        120 
AVANVELRYE EVNPYALLMP ASPHIAAEAE NVVIDYSVLS EGLASLKEKS DVVLVEGAGG 

       130        140        150        160        170        180 
WRVPVSKDDC LSTWVQQEKL PVVLVVGIKL GCLSHAMLTA EAIQHDGLEI IGWVANRVNP 

       190        200        210        220 
GTENYAEIIK MLEDKMPAPK LGEIPYMPSV KRKNMGKYIH LEALDN

« Hide

References

[1]"Complete sequence of Vibrio fischeri strain MJ11."
Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MJ11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001133 Genomic DNA. Translation: ACH64557.1.
RefSeqYP_002158415.1. NC_011186.1.

3D structure databases

ProteinModelPortalB5EUP7.
ModBaseSearch...

Protein-protein interaction databases

STRINGB5EUP7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6808615.
GenomeReviewsGene locus VFMJ11_A0867 in contig CP001133_GR.
KEGGvfm:VFMJ11_A0867.
PATRIC20125960. VBIVibFis37164_3603.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG650065.
OMAAEAVGWC.
ProtClustDBPRK00090.

Family and domain databases

HAMAPMF_00336. BioD.
[Tree]
InterProIPR002586. CbiA_P_synth.
IPR004472. DTB_synth_BioD.
[Graphical view]
KOK01935.
PfamPF01656. CbiA. 1 hit.
[Graphical view]
PIRSFPIRSF006755. DTB_synth. 1 hit.
TIGRFAMsTIGR00347. BioD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBIOD_VIBFM
AccessionPrimary (citable) accession number: B5EUP7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 14, 2008
Last modified: January 25, 2012
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents