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Q5L5F7 (BIOD_CHLAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 43. 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:CAB687
OrganismChlamydophila abortus [Complete proteome] [HAMAP]
Taxonomic identifier83555 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila

Protein attributes

Sequence length207 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 – 207207ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_1000133208

Regions

Nucleotide binding95 – 984ATP By similarity
Nucleotide binding155 – 1562ATP By similarity

Sites

Metal binding111Magnesium 1 By similarity
Metal binding151Magnesium 2 By similarity
Metal binding421Magnesium 2 By similarity
Metal binding951Magnesium 2 By similarity
Binding site351Substrate By similarity
Binding site421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5L5F7 [UniParc].

Last modified June 21, 2005. Version 1.
Checksum: 2794D7A5FE79FE15

FASTA20723,165
        10         20         30         40         50         60 
MHIIIAGIDT DVGKTFVSAI LTVLLQAEYW KPIQSGSLNH SDSAIVHALS GARCHPESYR 

        70         80         90        100        110        120 
FSHALAAHQA AQIDNITMHQ ETITLPKTDA SLIIETSGGF LSPCTHDSLQ GDVFAQWPCH 

       130        140        150        160        170        180 
WVLVSKAYLG SINHTCLTLE AMRARNLSIL GIILNQYPKE EEDWLLRTTG LPFLGRLNYE 

       190        200 
KSISKATVQN YANLWKETWK YRDTLLC 

« Hide

References

[1]"The Chlamydophila abortus genome sequence reveals an array of variable proteins that contribute to interspecies variation."
Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D., Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D., Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A., Price C., Barrell B.G., Parkhill J., Longbottom D.
Genome Res. 15:629-640(2005) [PubMed: 15837807] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S26/3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR848038 Genomic DNA. Translation: CAH64134.1.
RefSeqYP_220085.1. NC_004552.2.

3D structure databases

ProteinModelPortalQ5L5F7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3337274.
GenomeReviewsGene locus CAB687 in contig CR848038_GR.
KEGGcab:CAB687.
PATRIC20202897. VBIChlAbo21869_0752.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG650065.
OMAWKPIQSG.
ProtClustDBCLSK399497.

Enzyme and pathway databases

BioCycCABO218497:CAB687-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_CHLAB
AccessionPrimary (citable) accession number: Q5L5F7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 21, 2005
Last modified: January 25, 2012
This is version 43 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