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Q81MA9 (BIOD_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 63. 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:BA_4340, GBAA_4340, BAS4027
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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
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 – 242242ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000302475

Regions

Nucleotide binding12 – 176ATP By similarity
Nucleotide binding112 – 1154ATP By similarity

Sites

Metal binding121Magnesium 1 By similarity
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
Q81MA9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D77C9DFAD73D2D49

FASTA24226,294
        10         20         30         40         50         60 
MSGFFITATD TEVGKTVVAG ALAGVFRELG YNIGVYKALQ SGHVASNPEG DAARLKVLSG 

        70         80         90        100        110        120 
VPIKEDEICP YSIEEPLAPR LAMKRAGRAV TLKDIIHHYN ERLKEFNSLF VEGAGGLAVP 

       130        140        150        160        170        180 
YTEDALVIDF AKELQLPLIV VARPTLGTVN HTVLTIAYAK AHGLTVAGVI LSGCKECEME 

       190        200        210        220        230        240 
RVQENKVMIE ELSGVPVLGL LPFFEGEFTK EEVLESAKEY IMISKLEEFI RNESTVAHTS 


SN 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[3]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP28059.1.
AE017334 Genomic DNA. Translation: AAT33461.1.
AE017225 Genomic DNA. Translation: AAT56328.1.
RefSeqNP_846573.1. NC_003997.3.
YP_020986.1. NC_007530.2.
YP_030277.1. NC_005945.1.

3D structure databases

HSSPHSSP built from PDB template 1DAI based on UniProtKB P13000.
ProteinModelPortalQ81MA9.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000009382; EBBACP00000009138; EBBACG00000009374.
EBBACT00000014515; EBBACP00000014136; EBBACG00000014507.
EBBACT00000022127; EBBACP00000021612; EBBACG00000022118.
GeneID1087558.
2818966.
2852484.
GenomeReviewsGene locus BA_4340 in contig AE016879_GR.
Gene locus BAS4027 in contig AE017225_GR.
Gene locus GBAA_4340 in contig AE017334_GR.
KEGGban:BA_4340.
bar:GBAA_4340.
bat:BAS4027.
TIGRBA_4340.
GBAA_4340.

Phylogenomic databases

GeneTreeEBGT00050000001962.
HOGENOMHBG650065.
OMAANCVDPN.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycBANT260799:BAS4027-MONOMER.
BANT261594:GBAA4340-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_BACAN
AccessionPrimary (citable) accession number: Q81MA9
Secondary accession number(s): Q6HTR1, Q6KMZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2003
Last modified: December 14, 2011
This is version 63 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