Skip Header

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

Q9AMS4 (BIOD_BRAJA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. 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:blr2098
ORF Names:id903
OrganismBradyrhizobium japonicum
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Bradyrhizobium

Protein attributes

Sequence length211 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
Reference 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 – 211211ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000302482

Regions

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

Sites

Metal binding171Magnesium 2 By similarity
Metal binding471Magnesium 2 By similarity
Metal binding1011Magnesium 2 By similarity
Binding site1921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AMS4 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 2B81D4EE99CDBD2A

FASTA21123,218
        10         20         30         40         50         60 
MNKRIVVTGT DTGVGKTVFS AGLAGLLGAN YWKPVQAGLE QEIDSECIRR LGGLSSDRIV 

        70         80         90        100        110        120 
PELYRLRTPA SPHHSAEIDG VRIDTETLGL PDSGERRLVI EGAGGLMVPL TARTLYIDIF 

       130        140        150        160        170        180 
ERWQLPVVLC ARTGLGTINH SLLSIEALRK RQIRILGIAF IGERNAETES AVCEIGRVRW 

       190        200        210 
LGRLPWLVPL TNDRLQAAFK DSFVSSDFLN L

« Hide

References

« Hide 'large scale' references
[1]"Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA region of the Bradyrhizobium japonicum chromosome."
Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R., Hennecke H.
J. Bacteriol. 183:1405-1412(2001) [PubMed: 11157954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: USDA 110spc4.
[2]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF322013 Genomic DNA. Translation: AAG61073.1.
BA000040 Genomic DNA. Translation: BAC47363.1.
RefSeqNP_768738.1. NC_004463.1.

3D structure databases

HSSPHSSP built from PDB template 1DTS based on UniProtKB P13000.
ProteinModelPortalQ9AMS4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1055454.
GenomeReviewsGene locus blr2098 in contig BA000040_GR.
KEGGbja:blr2098.
NMPDRfig|224911.1.peg.2098.
PATRIC21187540. VBIBraJap65052_2032.

Phylogenomic databases

HOGENOMHBG650065.
OMAWKPIQSG.
PhylomeDBQ9AMS4.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycBJAP224911:BLR2098-MONOMER.

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_BRAJA
AccessionPrimary (citable) accession number: Q9AMS4
Secondary accession number(s): Q79UC2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2001
Last modified: January 25, 2012
This is version 61 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