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A5I426 (BIOD_CLOBH) 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:CBO2258, CLC_2182
OrganismClostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Taxonomic identifier441771 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length227 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
Reference 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 – 227227ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_1000019557

Regions

Nucleotide binding116 – 1194ATP By similarity
Nucleotide binding179 – 1802ATP 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

Sequences

Sequence LengthMass (Da)Tools
A5I426 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 3CEEEBE362A5C853

FASTA22725,363
        10         20         30         40         50         60 
MARGIFITAT GTDIGKTYVT ALIIKRLRET NINCGYYKAA LSGAERRDGK LIAGDANYVY 

        70         80         90        100        110        120 
NIANIKGDPN DAVSYIFQQA VSPHLAAKLN NVEISMERIK KDFYSIKNKY DYITVEGSGG 

       130        140        150        160        170        180 
IVCPISTGKE RIMLHNIIKI FKLPAIVVAD AGLGTINSTI LTLQYMKEKN ISVKMILLNN 

       190        200        210        220 
YNHKDIIHIE NKGYLSDNLL IPVYTCNKNA NNLEIPVEKL IEIYEEI 

« Hide

References

[1]"Genome sequence of a proteolytic (Group I) Clostridium botulinum strain Hall A and comparative analysis of the clostridial genomes."
Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G., Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L., Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M., Churcher C., Quail M.A., Chillingworth T. expand/collapse author list , Feltwell T., Fraser A., Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M., White B., Whithead S., Parkhill J.
Genome Res. 17:1082-1092(2007) [PubMed: 17519437] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.
[2]"Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within plasmids."
Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C., Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.
PLoS ONE 2:E1271-E1271(2007) [PubMed: 18060065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Hall / ATCC 3502 / NCTC 13319 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000727 Genomic DNA. Translation: ABS38852.1.
AM412317 Genomic DNA. Translation: CAL83797.1.
RefSeqYP_001254749.1. NC_009495.1.
YP_001388028.1. NC_009698.1.

3D structure databases

ProteinModelPortalA5I426.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5I426.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5186513.
5401450.
GenomeReviewsGene locus CBO2258 in contig AM412317_GR.
Gene locus CLC_2182 in contig CP000727_GR.
KEGGcbh:CLC_2182.
cbo:CBO2258.
PATRIC19366571. VBICloBot22612_2228.

Phylogenomic databases

eggNOGCOG0132.
HOGENOMHBG650065.
OMALNNYNHE.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycCBOT36826:CBO2258-MONOMER.
CBOT441771:CLC_2182-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_CLOBH
AccessionPrimary (citable) accession number: A5I426
Secondary accession number(s): A7G5G3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 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