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Q0I5V1 (SDHD_HAES1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:
Probable D-serine dehydratase

EC=4.3.1.18
Alternative name(s):
D-serine deaminase
Short name=DSD
Gene names
Name:dsdA
Ordered Locus Names:HS_1718
OrganismHaemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-serine = pyruvate + NH3. HAMAP MF_01030

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_01030

Sequence similarities

Belongs to the serine/threonine dehydratase family. DsdA subfamily.

Sequence caution

The sequence ABI25986.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processD-amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionD-serine ammonia-lyase activity

Inferred from electronic annotation. Source: EC

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Probable D-serine dehydratase HAMAP MF_01030
PRO_0000291732

Amino acid modifications

Modified residue1141N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I5V1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: DEB359375D95687C

FASTA43848,558
        10         20         30         40         50         60 
MKIQHLMQDP FIQKLMRFEE VMWFNPKSAG VKTGLSYVGL DVSDTQQAAE RLQRFAPYFC 

        70         80         90        100        110        120 
RAFPETQKTK GILESELVSI DKMKSALIDH YHMPIQGRLL LKKDSHLPIS GSIKARGGIY 

       130        140        150        160        170        180 
EVLAYAEKLA LEHHLITEND DYSQLCDEKI KDFFSRYSIA VGSTGNLGLS IGIMGAVLGF 

       190        200        210        220        230        240 
KVSVHMSADA REWKKQKLRS YGVNVVEYTQ DYGVAVAQGR KAALSDPNCF FIDDENSTTL 

       250        260        270        280        290        300 
FLGYSVAGQR LKQQFLEQGI KVDENHPLFV YLPCGVGGGP GGVAFGLKLA FGDYVHCIFA 

       310        320        330        340        350        360 
EPTHSPCMLL GVYTGLHDKI AVQDLGIDNI TAADGLAVGR ASGFVGRAME HLLDGFYTIE 

       370        380        390        400        410        420 
DQKLYDLLGL LHKTENIQLE PSALAGMIGP LHINHSDYLR RYHITQEQLA NATHIVWATG 

       430 
GGMVPDVEMQ KYLSLGRF 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed: 17172329] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25986.1. Different initiation.
RefSeqYP_719923.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I5V1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0I5V1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4241250.
GenomeReviewsGene locus HS_1718 in contig CP000436_GR.
KEGGhso:HS_1718.
NMPDRfig|205914.1.peg.1659.
PATRIC20283605. VBIHaeSom53361_1797.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3048.
HOGENOMHBG288722.
ProtClustDBPRK02991.

Enzyme and pathway databases

BioCycHSOM205914:HS_1718-MONOMER.

Family and domain databases

HAMAPMF_01030. D-Ser_dehydrat.
[Tree]
InterProIPR011780. D_Ser_am_lyase.
IPR001926. PyrdxlP-dep_enz_bsu.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
[Graphical view]
KOK01753.
PANTHERPTHR10314:SF9. D_Ser_am_lyase. 1 hit.
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR02035. D_Ser_am_lyase. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSDHD_HAES1
AccessionPrimary (citable) accession number: Q0I5V1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: January 25, 2012
This is version 34 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