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A3Q145 (BIOD_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Mjls_3093
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length229 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 – 229229ATP-dependent dethiobiotin synthetase BioD HAMAP MF_00336
PRO_0000302526

Regions

Nucleotide binding112 – 1154ATP By similarity
Nucleotide binding201 – 2033ATP By similarity

Sites

Metal binding161Magnesium 2 By similarity
Metal binding531Magnesium 2 By similarity
Metal binding1121Magnesium 2 By similarity
Binding site411Substrate By similarity
Binding site531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3Q145 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 6D8C7A617DA218CC

FASTA22922,806
        10         20         30         40         50         60 
MSVLVITGTD TGVGKTVATA ALACAARVAG IDVAVCKPVQ TGTGPAGGTG DDDLVEIGRL 

        70         80         90        100        110        120 
AGVDALHPGW RYPDPLAPVA AAERAGAALP TRDELIGMIR AADAPGRLTL VEGAGGLLVE 

       130        140        150        160        170        180 
LGQDAVTLRD VATELAAPVL VVVAPGLGTL NHTALTLESL AAQQVPCAGL VIGAWPAQPG 

       190        200        210        220 
AAEIDNRDAL ARLAPVRAAL PAGVGSVSPV DFERISATAF DPNWLAGLL

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000580 Genomic DNA. Translation: ABN98872.1.
RefSeqYP_001071363.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3Q145.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3Q145.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000051883; EBMYCP00000050164; EBMYCG00000051878.
GeneID4878806.
GenomeReviewsGene locus Mjls_3093 in contig CP000580_GR.
KEGGmjl:Mjls_3093.
PATRIC18092369. VBIMycSp51234_3114.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0132.
GeneTreeEBGT00050000017652.
HOGENOMHBG650065.
OMAAEAVGWC.
PhylomeDBA3Q145.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycMSP164757:MJLS_3093-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_MYCSJ
AccessionPrimary (citable) accession number: A3Q145
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 31 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

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