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Q2T1Q3 (BIOD_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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

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:BTH_I0338
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length240 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 – 240240ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000302494

Regions

Nucleotide binding118 – 1214ATP By similarity
Nucleotide binding178 – 1792ATP By similarity

Sites

Metal binding151Magnesium 1 By similarity
Metal binding191Magnesium 2 By similarity
Metal binding571Magnesium 2 By similarity
Metal binding1181Magnesium 2 By similarity
Binding site571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2T1Q3 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 71BA9D43748EA278

FASTA24024,955
        10         20         30         40         50         60 
MSAPLSLFVT GTDTEIGKTF VSTALLHGFA RAGLRAAAMK PIAAGAYQRD GVWRNEDADQ 

        70         80         90        100        110        120 
LDAAANVALP ATIRTPFLLK AAAAPHIAAA REGVALDIDT IVGAHRRACE RADVVVVEGV 

       130        140        150        160        170        180 
GGFRVPLAGT RDTADLAVAL GLPVVLVVGV RLGCISHALL TADAIAARGL AIAGWVANRV 

       190        200        210        220        230        240 
DAAMRFADDN VDTLRAWLER EHGAPLLGDI AHMSPPSPEA ASRSLDVNRL LGALRETAPR 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC39482.1.
RefSeqYP_440896.1. NC_007651.1.

3D structure databases

ProteinModelPortalQ2T1Q3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2T1Q3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3848467.
GenomeReviewsGene locus BTH_I0338 in contig CP000086_GR.
KEGGbte:BTH_I0338.
PATRIC19303364. VBIBurTha36512_3001.
TIGRBTH_I0338.

Phylogenomic databases

eggNOGCOG0132.
HOGENOMHBG650065.
OMAHRRACER.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I0338-MONOMER.

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_BURTA
AccessionPrimary (citable) accession number: Q2T1Q3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 39 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