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A5EFG7 (BIOD_BRASB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BBta_2778
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length210 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 – 210210ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000302483

Regions

Nucleotide binding101 – 1044ATP By similarity
Nucleotide binding185 – 1873ATP By similarity

Sites

Metal binding171Magnesium 2 By similarity
Metal binding1011Magnesium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
A5EFG7 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: CA1D1F2803AE6C29

FASTA21022,356
        10         20         30         40         50         60 
MAQRIVVTGT DTGIGKTVFA AALTDLLGAC YWKPVQAGLA EETDSHRVQR LADLADDRLV 

        70         80         90        100        110        120 
PEAYRLAAPA SPHLAARLDG VSIDPLCLNP PDTGGRPLVI EGAGGVMVPL TADTLYLDVF 

       130        140        150        160        170        180 
ARWQWPVVLC ARTSLGTINH SLLSLAALRS RGIAVLGVAF IGDANADSEE TICRLGAVKR 

       190        200        210 
LGRLPWLPEL TARSLQHAVA AEFRRADFAP 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000494 Genomic DNA. Translation: ABQ34911.1.
RefSeqYP_001238817.1. NC_009485.1.

3D structure databases

ProteinModelPortalA5EFG7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5EFG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5150932.
GenomeReviewsGene locus BBta_2778 in contig CP000494_GR.
KEGGbbt:BBta_2778.
PATRIC21206385. VBIBraSp29847_2875.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0132.
HOGENOMHBG650065.
OMAWKPIQSG.
ProtClustDBPRK00090.

Family and domain databases

HAMAPMF_00336. BioD.
[Tree]
InterProIPR004472. DTB_synth_BioD.
[Graphical view]
KOK01935.
PIRSFPIRSF006755. DTB_synth. 1 hit.
TIGRFAMsTIGR00347. BioD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBIOD_BRASB
AccessionPrimary (citable) accession number: A5EFG7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 12, 2007
Last modified: December 14, 2011
This is version 27 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