Skip Header

Contribute Send feedback
Read comments (?) or add your own

A8A0V7 (SELD_ECOHS) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Selenide, water dikinase
EC=2.7.9.3
Alternative name(s):
Selenium donor protein
Selenophosphate synthase
Gene names
Name:selD
Ordered Locus Names:EcHS_A1848
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Synthesizes selenophosphate from selenide and ATP By similarity. HAMAP MF_00625

Catalytic activity

ATP + selenide + H2O = AMP + selenophosphate + phosphate. HAMAP MF_00625

Cofactor

Magnesium By similarity. HAMAP MF_00625

Sequence similarities

Belongs to the selenophosphate synthase 1 family. Class I subfamily.

Ontologies

Keywords
   LigandATP-binding
Magnesium
Nucleotide-binding
Selenium
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

selenide, water dikinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 347347Selenide, water dikinase HAMAP MF_00625
PRO_0000318669

Regions

Nucleotide binding230 – 2367ATP Potential

Sites

Active site171 Potential
Site201Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A8A0V7 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 595E5EC9F7B1370F

FASTA34736,687
        10         20         30         40         50         60 
MSENSIRLTQ YSHGAGCGCK ISPKVLETIL HSEQAKFVDP NLLVGNETRD DAAVYDLGNG 

        70         80         90        100        110        120 
TSVISTTDFF MPIVDNPFDF GRIAATNAIS DIFAMGGKPI MAIAILGWPI NKLSPEIARE 

       130        140        150        160        170        180 
VTEGGRYACR QAGIALAGGH SIDAPEPIFG LAVTGIVPTE RVKKNSTAQA GCKLFLTKPL 

       190        200        210        220        230        240 
GIGVLTTAEK KSLLKPEHQG LATEVMCRMN IAGASFANIE GVKAMTDVTG FGLLGHLSEM 

       250        260        270        280        290        300 
CQGAGVQARV DYEAIPKLPG VEEYIKLGAV PGGTERNFAS YGHLMGEMPR EVRDLLCDPQ 

       310        320        330        340 
TSGGLLLAVM PEAENEVKAT AAEFGIELTA IGELVPARGG RAMVEIR

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000802 Genomic DNA. Translation: ABV06161.1.
RefSeqYP_001458544.1. NC_009800.1.

3D structure databases

ProteinModelPortalA8A0V7.
SMRA8A0V7. Positions 4-342.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8A0V7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000050760; EBESCP00000048745; EBESCG00000049808.
GeneID5591032.
GenomeReviewsGene locus EcHS_A1848 in contig CP000802_GR.
KEGGecx:EcHS_A1848.
PATRIC18313674. VBIEscCol77814_1808.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0709.
GeneTreeEBGT00050000011423.
HOGENOMHBG383791.
OMADYIAQGC.
ProtClustDBPRK00943.

Family and domain databases

HAMAPMF_00625. SelD.
[Tree]
InterProIPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR016188. PurM_N-like.
IPR004536. SelD.
IPR023061. SelD_I.
[Graphical view]
KOK01008.
PfamPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]
PIRSFPIRSF036407. Selenphspht_syn. 1 hit.
SUPFAMSSF56042. AIR_synth_C. 1 hit.
SSF55326. PurM_N-like. 1 hit.
TIGRFAMsTIGR00476. SelD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSELD_ECOHS
AccessionPrimary (citable) accession number: A8A0V7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 23, 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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents