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Q5HSS7 (SELD_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:CJE1677
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length340 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
   Coding sequence diversitySelenocysteine
   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 – 340340Selenide, water dikinase HAMAP MF_00625
PRO_1000051595

Regions

Nucleotide binding227 – 2337ATP Potential

Sites

Active site171 Potential
Site201Important for catalytic activity By similarity

Amino acid modifications

Non-standard residue171Selenocysteine Potential

Sequences

Sequence LengthMass (Da)Tools
Q5HSS7 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: 12259CB8C6B2D622

FASTA34037,194
        10         20         30         40         50         60 
MQYKNQNLTH FVKAAGUAAK LSPGGLKTIL NFMQKTPALL SDIGNNEDAS VYQISRDLAL 

        70         80         90        100        110        120 
VQTLDFITPI VDSAYHFGAI AAANALSDVF AMGAEVINAL NIVGFDTCNH DVNILKELLE 

       130        140        150        160        170        180 
GANDKVQECN ALVVGGHTIE STELFFGLSV TGKVHPSKFI ANNTSKIGDC IILTKPLGTG 

       190        200        210        220        230        240 
ILSTALKAQM LNQKHLDIML KNMMELNYKA SQIALKFHPS AMSDVTGFGL LGHLKEMLNK 

       250        260        270        280        290        300 
NISFEIFQNE ILFLEGAKEY FNMGLIPAGA YKNLEFIKEL IPDLNEEKLL LCDPQTSGGL 

       310        320        330        340 
LISISEKESL ECLKKLEDEN IQAKIIAKVV NKQENDIIIS

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000025 Genomic DNA. Translation: AAW36110.1.
RefSeqYP_179658.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HSS7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HSS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3232305.
GenomeReviewsGene locus CJE1677 in contig CP000025_GR.
KEGGcjr:CJE1677.
PATRIC20045149. VBICamJej134361_1687.
TIGRCJE1677.

Phylogenomic databases

eggNOGCOG0709.
HOGENOMHBG383791.
OMAAGXAAKL.
ProtClustDBCLSK879291.

Enzyme and pathway databases

BioCycCJEJ195099:CJE_1677-MONOMER.

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_CAMJR
AccessionPrimary (citable) accession number: Q5HSS7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 26, 2008
Last modified: January 25, 2012
This is version 41 of the entry and version 2 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

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