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Protein

D-serine dehydratase

Gene

dsdA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-serine = pyruvate + NH3.

Cofactori

GO - Molecular functioni

  • D-serine ammonia-lyase activity Source: CACAO
  • hydro-lyase activity Source: EcoliWiki
  • L-serine ammonia-lyase activity Source: GO_Central
  • pyridoxal phosphate binding Source: EcoCyc
  • serine racemase activity Source: GO_Central

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • detoxification of nitrogen compound Source: EcoCyc
  • D-serine biosynthetic process Source: GO_Central
  • D-serine catabolic process Source: EcoCyc
  • D-serine metabolic process Source: EcoliWiki
  • L-serine metabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:DSERDEAM-MONOMER.
ECOL316407:JW2363-MONOMER.
MetaCyc:DSERDEAM-MONOMER.
BRENDAi4.3.1.18. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
D-serine dehydratase (EC:4.3.1.18)
Alternative name(s):
D-serine deaminase
Short name:
DSD
Gene namesi
Name:dsdA
Ordered Locus Names:b2366, JW2363
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10249. dsdA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442D-serine dehydratasePRO_0000185611Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei118 – 1181N6-(pyridoxal phosphate)lysine

Proteomic databases

EPDiP00926.
PaxDbiP00926.
PRIDEiP00926.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4260555. 3 interactions.
IntActiP00926. 4 interactions.
STRINGi511145.b2366.

Structurei

Secondary structure

1
442
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 126Combined sources
Helixi15 – 206Combined sources
Beta strandi26 – 283Combined sources
Helixi35 – 384Combined sources
Helixi39 – 413Combined sources
Helixi46 – 6621Combined sources
Helixi68 – 736Combined sources
Beta strandi81 – 833Combined sources
Helixi85 – 9511Combined sources
Beta strandi101 – 1077Combined sources
Helixi108 – 1103Combined sources
Turni112 – 1143Combined sources
Helixi118 – 13619Combined sources
Helixi146 – 1505Combined sources
Helixi152 – 1598Combined sources
Beta strandi161 – 1666Combined sources
Helixi170 – 18213Combined sources
Beta strandi185 – 1917Combined sources
Helixi196 – 2049Combined sources
Beta strandi208 – 2147Combined sources
Helixi216 – 22813Combined sources
Beta strandi233 – 2353Combined sources
Turni238 – 2403Combined sources
Helixi242 – 2498Combined sources
Helixi251 – 26212Combined sources
Beta strandi272 – 2776Combined sources
Beta strandi279 – 2813Combined sources
Helixi282 – 29514Combined sources
Helixi296 – 2983Combined sources
Beta strandi299 – 3068Combined sources
Helixi311 – 3188Combined sources
Helixi321 – 3233Combined sources
Helixi326 – 3294Combined sources
Helixi338 – 3403Combined sources
Helixi349 – 3535Combined sources
Helixi354 – 3563Combined sources
Beta strandi359 – 3635Combined sources
Helixi365 – 37915Combined sources
Helixi385 – 3928Combined sources
Helixi393 – 3997Combined sources
Helixi401 – 4077Combined sources
Helixi411 – 4155Combined sources
Beta strandi418 – 4236Combined sources
Helixi431 – 44010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SS7X-ray1.55X1-442[»]
3SS9X-ray1.97X1-442[»]
ProteinModelPortaliP00926.
SMRiP00926. Positions 6-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105BZC. Bacteria.
COG3048. LUCA.
HOGENOMiHOG000218072.
InParanoidiP00926.
KOiK01753.
OMAiESDPNCF.
PhylomeDBiP00926.

Family and domain databases

HAMAPiMF_01030. D_Ser_dehydrat. 1 hit.
InterProiIPR011780. D_Ser_am_lyase.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PANTHERiPTHR10314:SF9. PTHR10314:SF9. 2 hits.
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR02035. D_Ser_am_lyase. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00926-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENAKMNSLI AQYPLVKDLV ALKETTWFNP GTTSLAEGLP YVGLTEQDVQ
60 70 80 90 100
DAHARLSRFA PYLAKAFPET AATGGIIESE LVAIPAMQKR LEKEYQQPIS
110 120 130 140 150
GQLLLKKDSH LPISGSIKAR GGIYEVLAHA EKLALEAGLL TLDDDYSKLL
160 170 180 190 200
SPEFKQFFSQ YSIAVGSTGN LGLSIGIMSA RIGFKVTVHM SADARAWKKA
210 220 230 240 250
KLRSHGVTVV EYEQDYGVAV EEGRKAAQSD PNCFFIDDEN SRTLFLGYSV
260 270 280 290 300
AGQRLKAQFA QQGRIVDADN PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH
310 320 330 340 350
CFFAEPTHSP CMLLGVHTGL HDQISVQDIG IDNLTAADGL AVGRASGFVG
360 370 380 390 400
RAMERLLDGF YTLSDQTMYD MLGWLAQEEG IRLEPSALAG MAGPQRVCAS
410 420 430 440
VSYQQMHGFS AEQLRNTTHL VWATGGGMVP EEEMNQYLAK GR
Length:442
Mass (Da):47,901
Last modified:November 1, 1997 - v3
Checksum:i3BCB9397AC8C7971
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341S → T AA sequence (PubMed:9222324).Curated
Sequence conflicti204 – 2041S → T in AAA87975 (PubMed:3053699).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01603 Genomic DNA. Translation: AAA87975.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC75425.1.
AP009048 Genomic DNA. Translation: BAA16229.1.
X86379 Genomic DNA. Translation: CAA60139.1.
PIRiC65010. DWECS.
RefSeqiNP_416867.1. NC_000913.3.
WP_000426427.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75425; AAC75425; b2366.
BAA16229; BAA16229; BAA16229.
GeneIDi946837.
KEGGiecj:JW2363.
eco:b2366.
PATRICi32120111. VBIEscCol129921_2464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01603 Genomic DNA. Translation: AAA87975.1. Sequence problems.
U00096 Genomic DNA. Translation: AAC75425.1.
AP009048 Genomic DNA. Translation: BAA16229.1.
X86379 Genomic DNA. Translation: CAA60139.1.
PIRiC65010. DWECS.
RefSeqiNP_416867.1. NC_000913.3.
WP_000426427.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SS7X-ray1.55X1-442[»]
3SS9X-ray1.97X1-442[»]
ProteinModelPortaliP00926.
SMRiP00926. Positions 6-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260555. 3 interactions.
IntActiP00926. 4 interactions.
STRINGi511145.b2366.

Proteomic databases

EPDiP00926.
PaxDbiP00926.
PRIDEiP00926.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75425; AAC75425; b2366.
BAA16229; BAA16229; BAA16229.
GeneIDi946837.
KEGGiecj:JW2363.
eco:b2366.
PATRICi32120111. VBIEscCol129921_2464.

Organism-specific databases

EchoBASEiEB0245.
EcoGeneiEG10249. dsdA.

Phylogenomic databases

eggNOGiENOG4105BZC. Bacteria.
COG3048. LUCA.
HOGENOMiHOG000218072.
InParanoidiP00926.
KOiK01753.
OMAiESDPNCF.
PhylomeDBiP00926.

Enzyme and pathway databases

BioCyciEcoCyc:DSERDEAM-MONOMER.
ECOL316407:JW2363-MONOMER.
MetaCyc:DSERDEAM-MONOMER.
BRENDAi4.3.1.18. 2026.

Miscellaneous databases

PROiP00926.

Family and domain databases

HAMAPiMF_01030. D_Ser_dehydrat. 1 hit.
InterProiIPR011780. D_Ser_am_lyase.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PANTHERiPTHR10314:SF9. PTHR10314:SF9. 2 hits.
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR02035. D_Ser_am_lyase. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSDHD_ECOLI
AccessioniPrimary (citable) accession number: P00926
Secondary accession number(s): P78303
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.