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A7Z5B3 (BIOD_BACA2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:RBAM_018260
OrganismBacillus amyloliquefaciens (strain FZB42) [Complete proteome] [HAMAP]
Taxonomic identifier326423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length233 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 – 233233ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_1000019548

Regions

Nucleotide binding112 – 1154ATP By similarity
Nucleotide binding202 – 2043ATP By similarity

Sites

Metal binding161Magnesium 2 By similarity
Metal binding511Magnesium 2 By similarity
Metal binding1121Magnesium 2 By similarity
Binding site411Substrate By similarity
Binding site511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A7Z5B3 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 35AA3F29E6E77F17

FASTA23325,540
        10         20         30         40         50         60 
MRSFFVTGTD TGVGKTIVSC GLAAAFRQKQ ADIGVFKPFL SGVPRTHPES DTSLLKDMSQ 

        70         80         90        100        110        120 
TALSHEEITP FEWKEPLAPY TAAMLEGKSV SMADVMAHWS KIKNRHECFI VEGAGGISVP 

       130        140        150        160        170        180 
LGENYLVSDL IKAMELPAVI VTRPDLGTIN HTYLTVEYAK NMGIEVLGII INGVRSRPGL 

       190        200        210        220        230 
DEKTNPSMIE TLCKVPILGI TPKLDHVSSE NIQHMIEKHI DVSSFMNLTQ MGR 

« Hide

References

[1]"Comparative analysis of the complete genome sequence of the plant growth-promoting bacterium Bacillus amyloliquefaciens FZB42."
Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K., Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H., Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H., Strittmatter A., Gottschalk G., Borriss R.
Nat. Biotechnol. 25:1007-1014(2007) [PubMed: 17704766] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FZB42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000560 Genomic DNA. Translation: ABS74189.1.
RefSeqYP_001421420.1. NC_009725.1.

3D structure databases

ProteinModelPortalA7Z5B3.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7Z5B3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000006893; EBBACP00000006771; EBBACG00000006885.
GeneID5459522.
GenomeReviewsGene locus RBAM_018260 in contig CP000560_GR.
KEGGbay:RBAM_018260.
PATRIC18748726. VBIBacAmy31356_1839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0132.
GeneTreeEBGT00050000001962.
HOGENOMHBG650065.
OMAPQMERIE.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycBAMY326423:RBAM_018260-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_BACA2
AccessionPrimary (citable) accession number: A7Z5B3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 30 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