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B7MY25 (SDHD_ECO81) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 29. 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:
D-serine dehydratase

EC=4.3.1.18
Alternative name(s):
D-serine deaminase
Short name=DSD
Gene names
Name:dsdA
Ordered Locus Names:ECED1_2813
OrganismEscherichia coli O81 (strain ED1a) [Complete proteome] [HAMAP]
Taxonomic identifier585397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length442 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-serine = pyruvate + NH3. HAMAP-Rule MF_01030

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01030

Subunit structure

Monomer By similarity. HAMAP-Rule MF_01030

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 442442D-serine dehydratase HAMAP-Rule MF_01030
PRO_1000149388

Amino acid modifications

Modified residue1181N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B7MY25 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 19AEB9B1CA573271

FASTA44247,837
        10         20         30         40         50         60 
MENAKMNSLI AQYPLVEDLV ALKETTWFNP GTTSLAEGLP YVGLTEQDVQ DAHARLSRFA 

        70         80         90        100        110        120 
PYLAKAFPET AAAGGIIESE LVAIPAMQKR LEKEYQQPIS GQLLLKKDSH LPISGSIKAR 

       130        140        150        160        170        180 
GGIYEVLAHA EKLALEAGLL TLEDDYSKLL SPEFKQFFSQ YSIAVGSTGN LGLSIGIMSA 

       190        200        210        220        230        240 
RIGFKVTVHM SADARAWKKA KLRSHGVTVV EYEQDYGVAV EEGRKAAQSD PNCFFIDDEN 

       250        260        270        280        290        300 
SRTLFLGYSV AGQRLKAQFA QQGRIVDADN PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH 

       310        320        330        340        350        360 
CFFAEPTHSP CMLLGVHTGL HDQISVQDIG IDNLTAADGL AVGRASGFVG RAMERLLDGF 

       370        380        390        400        410        420 
YTLSDQTMYD MLGWLAQEEG IRLEPSALAG MAGPQRVCAS VSYQQLHGFS AEQLRNATHL 

       430        440 
VWATGGGMVP EEEMNQYLAK GR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU928162 Genomic DNA. Translation: CAR08991.2.
RefSeqYP_002398721.1. NC_011745.1.

3D structure databases

ProteinModelPortalB7MY25.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR08991; CAR08991; ECED1_2813.
GeneID7140527.
KEGGecq:ECED1_2813.
PATRIC38489650. VBIEscCol8292_2818.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3048.
HOGENOMHOG000218072.
KOK01753.
OMAHCLFAEP.
ProtClustDBPRK02991.

Enzyme and pathway databases

BioCycECOL585397:GJCU-2845-MONOMER.

Family and domain databases

HAMAPMF_01030. D-Ser_dehydrat.
InterProIPR011780. D_Ser_am_lyase.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PANTHERPTHR10314:SF9. PTHR10314:SF9. 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_ECO81
AccessionPrimary (citable) accession number: B7MY25
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 29 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