Skip Header

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

Q9KER6 (BIOD_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. 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:BH0783
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length242 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 – 242242ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000187946

Regions

Nucleotide binding15 – 206ATP By similarity
Nucleotide binding117 – 1204ATP By similarity
Nucleotide binding178 – 1792ATP By similarity
Nucleotide binding208 – 2103ATP By similarity

Sites

Metal binding151Magnesium 1 By similarity
Metal binding191Magnesium 2 By similarity
Metal binding571Magnesium 2 By similarity
Metal binding1171Magnesium 2 By similarity
Binding site441Substrate By similarity
Binding site571ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KER6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 30D1730006201DD3

FASTA24227,115
        10         20         30         40         50         60 
MVIIRSFFIT GTDTDVGKTV VTSLLTRFLI DMGVNAFPYK PVQSGATTNG ARMIPSDAQM 

        70         80         90        100        110        120 
YQLVRPEFDV TDFNTYLLEK PCSPHLAADL ANITLDRTVI TKQVHQLEEA HDAVLIEGAG 

       130        140        150        160        170        180 
GLYVPLTNDG YCYIDFMEEL NVPTILVSAL RVGTINHTVL SIEAMKARNL PIAGIIFNQL 

       190        200        210        220        230        240 
QIGNPVIEQS NVETIRKLTD TPILGFVPYS PDIHTVLADD KLRRHLYKDW DKRRFKELIH 


SD

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000004 Genomic DNA. Translation: BAB04502.1.
PIRG83747.
RefSeqNP_241649.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KER6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000052149; EBBACP00000050788; EBBACG00000052140.
GeneID892858.
GenomeReviewsGene locus BH0783 in contig BA000004_GR.
KEGGbha:BH0783.
NMPDRfig|272558.1.peg.783.
PATRIC18938566. VBIBacHal18977_0821.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001962.
HOGENOMHBG650065.
OMALNNYNHE.
PhylomeDBQ9KER6.
ProtClustDBCLSK2393026.

Enzyme and pathway databases

BioCycBHAL272558:BH0783-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_BACHD
AccessionPrimary (citable) accession number: Q9KER6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 68 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