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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
  • D-amino acid metabolic process Source: UniProtKB-HAMAP
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001856111 – 442D-serine dehydrataseAdd BLAST442

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei118N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiP00926.
PaxDbiP00926.
PRIDEiP00926.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4260555. 3 interactors.
IntActiP00926. 4 interactors.
STRINGi511145.b2366.

Structurei

Secondary structure

1442
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 12Combined sources6
Helixi15 – 20Combined sources6
Beta strandi26 – 28Combined sources3
Helixi35 – 38Combined sources4
Helixi39 – 41Combined sources3
Helixi46 – 66Combined sources21
Helixi68 – 73Combined sources6
Beta strandi81 – 83Combined sources3
Helixi85 – 95Combined sources11
Beta strandi101 – 107Combined sources7
Helixi108 – 110Combined sources3
Turni112 – 114Combined sources3
Helixi118 – 136Combined sources19
Helixi146 – 150Combined sources5
Helixi152 – 159Combined sources8
Beta strandi161 – 166Combined sources6
Helixi170 – 182Combined sources13
Beta strandi185 – 191Combined sources7
Helixi196 – 204Combined sources9
Beta strandi208 – 214Combined sources7
Helixi216 – 228Combined sources13
Beta strandi233 – 235Combined sources3
Turni238 – 240Combined sources3
Helixi242 – 249Combined sources8
Helixi251 – 262Combined sources12
Beta strandi272 – 277Combined sources6
Beta strandi279 – 281Combined sources3
Helixi282 – 295Combined sources14
Helixi296 – 298Combined sources3
Beta strandi299 – 306Combined sources8
Helixi311 – 318Combined sources8
Helixi321 – 323Combined sources3
Helixi326 – 329Combined sources4
Helixi338 – 340Combined sources3
Helixi349 – 353Combined sources5
Helixi354 – 356Combined sources3
Beta strandi359 – 363Combined sources5
Helixi365 – 379Combined sources15
Helixi385 – 392Combined sources8
Helixi393 – 399Combined sources7
Helixi401 – 407Combined sources7
Helixi411 – 415Combined sources5
Beta strandi418 – 423Combined sources6
Helixi431 – 440Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SS7X-ray1.55X1-442[»]
3SS9X-ray1.97X1-442[»]
ProteinModelPortaliP00926.
SMRiP00926.
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)DescriptionActionsGraphical viewLength
Sequence conflicti34S → T AA sequence (PubMed:9222324).Curated1
Sequence conflicti204S → T in AAA87975 (PubMed:3053699).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SS7X-ray1.55X1-442[»]
3SS9X-ray1.97X1-442[»]
ProteinModelPortaliP00926.
SMRiP00926.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260555. 3 interactors.
IntActiP00926. 4 interactors.
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: November 2, 2016
This is version 138 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.