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B2JKH5 (BIOD_BURP8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:Bphy_0171
OrganismBurkholderia phymatum (strain DSM 17167 / STM815) [Complete proteome] [HAMAP]
Taxonomic identifier391038 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

Protein attributes

Sequence length239 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 – 239239ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_1000119864

Regions

Nucleotide binding15 – 206ATP By similarity
Nucleotide binding118 – 1214ATP By similarity
Nucleotide binding178 – 1792ATP By similarity
Nucleotide binding211 – 2133ATP 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
B2JKH5 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 3F101BB2DF5D9C2F

FASTA23925,193
        10         20         30         40         50         60 
MSPALSLFVT GTDTEIGKTL VSAALLRGFV RDGLRAAAMK PIAAGATLVN GVLHNEDADQ 

        70         80         90        100        110        120 
LDAAANVLLP PDIRTPFMLK EPAAPHIAAA HESVTLDMAR IVDAHEAALQ MADVVVVEGV 

       130        140        150        160        170        180 
GGFRVPLTDS HDTADLAFAL NLPVVLVVGM RLGCISHALL TAEAIAARGL RVVGWVANRV 

       190        200        210        220        230 
DPAMLFPDEN IDTLRDRLAR QYDAPLLGSV PHLSPASPDV AATHLDTTRL LHALRTAPR

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phymatum STM815."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Bruce D., Goodwin L., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Bacher J., Blanchard J., Cohan F., James E., Lawrence J., Lizotte-Waniewski M., Moulin L., Rainey P., Riley M., Souza V., Wertz J., Young P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17167 / STM815.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001043 Genomic DNA. Translation: ACC69364.1.
RefSeqYP_001856410.1. NC_010622.1.

3D structure databases

ProteinModelPortalB2JKH5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2JKH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6241673.
GenomeReviewsGene locus Bphy_0171 in contig CP001043_GR.
KEGGbph:Bphy_0171.
PATRIC19186451. VBIBurPhy25146_0184.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG650065.
OMAANCVDPN.
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_BURP8
AccessionPrimary (citable) accession number: B2JKH5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: January 25, 2012
This is version 28 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

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