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A1UHM2 (BIOD_MYCSK) 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:Mkms_3136
OrganismMycobacterium sp. (strain KMS) [Complete proteome] [HAMAP]
Taxonomic identifier189918 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

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_0000302527

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
A1UHM2 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 34402F6B0F106AC7

FASTA22922,903
        10         20         30         40         50         60 
MSVLVITGTD TGVGKTVATA ALACAARVAG IDVAVCKPVQ TGTGPVGGTG DDDLVEIGRL 

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

       130        140        150        160        170        180 
LGQDAVTLRD VATELDAPVL VVVAPGLGTL NHTALTLESL AAQHVPCAGL VIGAWPAQPG 

       190        200        210        220 
AAEIDNRDTL ARLAPVRAAL PAGVGSVSPV DFERISATAF DPNWLAGLL 

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. KMS."
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KMS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000518 Genomic DNA. Translation: ABL92330.1.
RefSeqYP_939120.1. NC_008705.1.

3D structure databases

ProteinModelPortalA1UHM2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1UHM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000058270; EBMYCP00000056494; EBMYCG00000058265.
GeneID4610971.
GenomeReviewsGene locus Mkms_3136 in contig CP000518_GR.
KEGGmkm:Mkms_3136.
PATRIC18105254. VBIMycSp70743_3658.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0132.
GeneTreeEBGT00050000017652.
HOGENOMHBG650065.
OMAAEAVGWC.
ProtClustDBPRK00090.

Enzyme and pathway databases

BioCycMSP189918:MKMS_3136-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_MYCSK
AccessionPrimary (citable) accession number: A1UHM2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: February 6, 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