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A0PYU7 (BIOD_CLONN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 32. 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:NT01CX_1468
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length238 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 – 238238ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000302498

Regions

Nucleotide binding116 – 1194ATP By similarity
Nucleotide binding209 – 2113ATP By similarity

Sites

Metal binding131Magnesium 1 By similarity
Metal binding171Magnesium 2 By similarity
Metal binding551Magnesium 2 By similarity
Metal binding1161Magnesium 2 By similarity
Binding site421Substrate By similarity
Binding site551ATP By similarity
Binding site2161ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PYU7 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 7744532A3DF52DA2

FASTA23826,249
        10         20         30         40         50         60 
MSNGIFIVGT DTDIGKTFVT GGILYLLRKN GVNASYFKAA LSGAIKVNER LIPGDTKFVS 

        70         80         90        100        110        120 
DLSGLNEEYS FLTPYVFETA VSPHLASKIE NIPINLEVIK SSYLKVKEKY DYIVAEGSGG 

       130        140        150        160        170        180 
IVCPMVHNEK STILLEDIIK LLDLDTLLVA SAGLGSINHT VLTVKYIENA GLNIKGIIVN 

       190        200        210        220        230 
GYDENNICHR DNVKMIKKLT SKDIIALIPR IKDNNNHKEI KKVFDDLDYK KIKKCIGA 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed: 17115055] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK61999.1.
RefSeqYP_877549.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0PYU7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PYU7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4539917.
GenomeReviewsGene locus NT01CX_1468 in contig CP000382_GR.
KEGGcno:NT01CX_1468.
PATRIC19478592. VBICloNov112828_0574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0132.
HOGENOMHBG650065.
OMAPQMERIE.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycCNOV386415:NT01CX_1468-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_CLONN
AccessionPrimary (citable) accession number: A0PYU7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 32 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