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Q76EQ0 (SRR_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine racemase

EC=4.3.1.17
EC=4.3.1.18
EC=5.1.1.18
Alternative name(s):
D-serine ammonia-lyase
D-serine dehydratase
L-serine ammonia-lyase
L-serine dehydratase
Gene names
Name:Srr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. Ref.3 Ref.4

Catalytic activity

L-serine = D-serine. Ref.4

L-serine = pyruvate + NH3. Ref.4

D-serine = pyruvate + NH3. Ref.4

Cofactor

Pyridoxal phosphate. Ref.4

Enzyme regulation

Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP By similarity. Competitively inhibited by malonate. Ref.4

Subunit structure

Homodimer. Ref.4

Post-translational modification

S-nitrosylated, leading to decrease the enzyme activity By similarity.

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Biophysicochemical properties

Kinetic parameters:

KM=3.7 mM for L-serine Ref.4

Ontologies

Keywords
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Pyridoxal phosphate
   Molecular functionIsomerase
Lyase
   PTMS-nitrosylation
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-serine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

D-serine metabolic process

Inferred from direct assay Ref.4. Source: UniProtKB

L-serine metabolic process

Inferred from direct assay Ref.4. Source: UniProtKB

aging

Inferred from expression pattern PubMed 16842499. Source: RGD

brain development

Inferred from expression pattern PubMed 16739185. Source: RGD

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

pyruvate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 17109841. Source: RGD

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from expression pattern PubMed 18603832. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 16716293. Source: RGD

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 16289842. Source: RGD

cytoplasm

Inferred from direct assay PubMed 16289842. Source: RGD

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 16289842. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay Ref.4. Source: UniProtKB

D-serine ammonia-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

L-serine ammonia-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

glycine binding

Inferred from electronic annotation. Source: Ensembl

magnesium ion binding

Inferred from direct assay Ref.4. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.4. Source: UniProtKB

pyridoxal phosphate binding

Inferred from direct assay Ref.4. Source: UniProtKB

serine racemase activity

Inferred from direct assay Ref.4. Source: UniProtKB

threonine racemase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Serine racemase
PRO_0000286173

Regions

Region238 – 2392Substrate binding By similarity

Sites

Active site561Proton acceptor By similarity
Active site841Proton acceptor By similarity
Metal binding2101Magnesium By similarity
Metal binding2141Magnesium; via carbonyl oxygen
Metal binding2161Magnesium By similarity
Binding site511ATP By similarity
Binding site1211ATP By similarity
Binding site1351Substrate Probable

Amino acid modifications

Modified residue561N6-(pyridoxal phosphate)lysine
Modified residue1131S-nitrosocysteine By similarity

Secondary structure

.......................................................... 333
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q76EQ0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B0DDD8B7B5A8116C

FASTA33335,693
        10         20         30         40         50         60 
MCAQYCISFA DVEKAHLNIQ DSVHLTPVLT SSILNQIAGR NLFFKCELFQ KTGSFKIRGA 

        70         80         90        100        110        120 
LNAIRGLIPD TLEGKPKAVV THSSGNHGQA LTYAAKLEGI PAYIVVPQTA PNCKKLAIQA 

       130        140        150        160        170        180 
YGASIVYSEP SDESRENVAQ RIIQETEGIL VHPNQEPAVI AGQGTIALEV LNQVPLVDAL 

       190        200        210        220        230        240 
VVPVGGGGMV AGIAITIKTL KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV 

       250        260        270        280        290        300 
KSSIGLNTWP IIRDLVDDVF TVTEDEIKYA TQLVWERMKL LIEPTAGVGL AAVLSQHFQT 

       310        320        330 
VSPEVKNICI VLSGGNVDLT SLSWVKQAER PAP 

« Hide

References

« Hide 'large scale' references
[1]"Rat cerebral serine racemase: amino acid deletion and truncation at carboxy terminus."
Konno R.
Neurosci. Lett. 349:111-114(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[3]"Glia-derived D-serine controls NMDA receptor activity and synaptic memory."
Panatier A., Theodosis D.T., Mothet J.P., Touquet B., Pollegioni L., Poulain D.A., Oliet S.H.
Cell 125:775-784(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding."
Smith M.A., Mack V., Ebneth A., Moraes I., Felicetti B., Wood M., Schonfeld D., Mather O., Cesura A., Barker J.
J. Biol. Chem. 285:12873-12881(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 3-333 IN COMPLEX WITH MANGANESE IONS; MALONATE AND PYRIDOXAL PHOSPHATE, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB106282 mRNA. Translation: BAC84968.1.
BC082014 mRNA. Translation: AAH82014.1.
RefSeqNP_942052.1. NM_198757.2.
UniGeneRn.220332.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3HMKX-ray2.10A/B1-333[»]
3L6CX-ray2.20A/B1-333[»]
ProteinModelPortalQ76EQ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000050774.

PTM databases

PhosphoSiteQ76EQ0.

Proteomic databases

PaxDbQ76EQ0.
PRIDEQ76EQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000046110; ENSRNOP00000050774; ENSRNOG00000002991.
GeneID303306.
KEGGrno:303306.

Organism-specific databases

CTD63826.
RGD735094. Srr.

Phylogenomic databases

eggNOGCOG1171.
GeneTreeENSGT00550000075026.
HOGENOMHOG000046974.
HOVERGENHBG023167.
InParanoidQ76EQ0.
KOK12235.
OMANIGPNTW.
OrthoDBEOG7HB5B2.
PhylomeDBQ76EQ0.
TreeFamTF313346.

Enzyme and pathway databases

BRENDA5.1.1.18. 5301.

Gene expression databases

GenevestigatorQ76EQ0.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ76EQ0.
NextBio651104.
PROQ76EQ0.

Entry information

Entry nameSRR_RAT
AccessionPrimary (citable) accession number: Q76EQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references