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P0A6F0 (BIOD2_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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 2
EC=6.3.3.3
Alternative name(s):
DTB synthetase 2
Short name=DTBS 2
Dethiobiotin synthase 2
Gene names
Name:bioD2
Synonyms:ynfK
Ordered Locus Names:Z2585, ECs2299
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length231 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

Subunit structure

Homodimer By similarity. HAMAP MF_00336

Subcellular location

Cytoplasm By similarity HAMAP MF_00336.

Sequence similarities

Belongs to the dethiobiotin synthetase family.

Sequence caution

The sequence AAG56580.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB35722.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 – 231231ATP-dependent dethiobiotin synthetase BioD 2 HAMAP MF_00336
PRO_0000187964

Regions

Nucleotide binding13 – 186ATP By similarity
Nucleotide binding112 – 1154ATP By similarity
Nucleotide binding172 – 1732ATP By similarity
Nucleotide binding201 – 2033ATP By similarity

Sites

Metal binding171Magnesium 2 By similarity
Metal binding551Magnesium 2 By similarity
Metal binding1121Magnesium 2 By similarity
Binding site551ATP By similarity
Binding site2081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A6F0 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 35A04911309A99B0

FASTA23124,981
        10         20         30         40         50         60 
MLKRFFITGT DTSVGKTVVS RALLQALASQ GKTVAGYKPV AKGSKETPEG LRNKDALVLQ 

        70         80         90        100        110        120 
SVSTIELPYE AVNPIALSEE ESSVAHSCPI NYTLISNGLA NLTEKVDHVV VEGTGGWRSL 

       130        140        150        160        170        180 
MNDLRPLSEW VVQEQLPVLM VVGIQEGCIN HALLTAQAIA NDGLPLIGWV ANRINPGLAH 

       190        200        210        220        230 
YAEIIDVLGK KLPAPLIGEL PYLPRAEQRE LGQYIRLAML RSVLAVDRVT V

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE005174 Genomic DNA. Translation: AAG56580.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB35722.1. Different initiation.
RefSeqNP_288028.2. NC_002655.2.
NP_310326.2. NC_002695.1.

3D structure databases

ProteinModelPortalP0A6F0.
SMRP0A6F0. Positions 2-220.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000027347; EBESCP00000026240; EBESCG00000026399.
EBESCT00000057484; EBESCP00000055312; EBESCG00000056532.
GeneID913895.
961539.
GenomeReviewsGene locus Z2585 in contig AE005174_GR.
Gene locus ECs2299 in contig BA000007_GR.
KEGGece:Z2585.
ecs:ECs2299.
PATRIC18353924. VBIEscCol44059_2175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010427.
HOGENOMHBG650065.
OMATRTNEDV.
ProtClustDBPRK12374.

Enzyme and pathway databases

BioCycECOL83334:ECS2299-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 nameBIOD2_ECO57
AccessionPrimary (citable) accession number: P0A6F0
Secondary accession number(s): P77201, Q8X788
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: January 25, 2012
This is version 45 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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