Skip Header

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

Q8FWG5 (BIOD_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BRA0490, BS1330_II0486
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length212 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 – 212212ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000187951

Regions

Nucleotide binding100 – 1034ATP By similarity
Nucleotide binding184 – 1863ATP By similarity

Sites

Metal binding171Magnesium 2 By similarity
Metal binding1001Magnesium 2 By similarity
Binding site371Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FWG5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F7D5083F8F33E1DC

FASTA21222,988
        10         20         30         40         50         60 
MNSRLIVTGT DTGIGKTVFS AALCHALGAA YWKPVQSGLE EETDSEIVAR LAQASPQRIL 

        70         80         90        100        110        120 
PEAWRLNTPA SPHLSARLDG VEIRPEEMHI PATSLPLVIE GAGGLLVPLN DKTLFADLFA 

       130        140        150        160        170        180 
IWRIPAILCA RAALGTINHT LLSLEAMRSR DIPVLGVAFI GEANEDTETT IAHLGRVKRL 

       190        200        210 
GRLPLLDDLS PEKLHHSFAR NFHIDDFAGV AR 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014292 Genomic DNA. Translation: AAN33682.1.
CP002998 Genomic DNA. Translation: AEM19960.1.
RefSeqNP_699677.1. NC_004311.2.

3D structure databases

ProteinModelPortalQ8FWG5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1164928.
GenomeReviewsGene locus BRA0490 in contig AE014292_GR.
KEGGbms:BRA0490.
NMPDRfig|204722.1.peg.2586.
PATRIC17793789. VBIBruSui107850_2710.
TIGRBRA0490.

Phylogenomic databases

HOGENOMHBG650065.
OMAWKPIQSG.
PhylomeDBQ8FWG5.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycBSUI204722:BR_A0490-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_BRUSU
AccessionPrimary (citable) accession number: Q8FWG5
Secondary accession number(s): G0KCM2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella suis

Brucella suis (strain 1330): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families