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Q76EQ0

- SRR_RAT

UniProt

Q76EQ0 - SRR_RAT

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Protein
Serine racemase
Gene
Srr
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

L-serine = D-serine.1 Publication
L-serine = pyruvate + NH3.1 Publication
D-serine = pyruvate + NH3.1 Publication

Cofactori

Pyridoxal phosphate.1 Publication

Enzyme regulationi

Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP By similarity. Competitively inhibited by malonate.1 Publication

Kineticsi

  1. KM=3.7 mM for L-serine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATP By similarity
Active sitei56 – 561Proton acceptor By similarity
Active sitei84 – 841Proton acceptor By similarity
Binding sitei121 – 1211ATP By similarity
Binding sitei135 – 1351Substrate Inferred
Metal bindingi210 – 2101Magnesium By similarity
Metal bindingi214 – 2141Magnesium; via carbonyl oxygen
Metal bindingi216 – 2161Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. D-serine ammonia-lyase activity Source: UniProtKB-EC
  3. L-serine ammonia-lyase activity Source: UniProtKB-EC
  4. calcium ion binding Source: Ensembl
  5. glycine binding Source: Ensembl
  6. magnesium ion binding Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB
  8. pyridoxal phosphate binding Source: UniProtKB
  9. serine racemase activity Source: UniProtKB
  10. threonine racemase activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. D-serine biosynthetic process Source: Ensembl
  2. D-serine metabolic process Source: UniProtKB
  3. L-serine metabolic process Source: UniProtKB
  4. aging Source: RGD
  5. brain development Source: RGD
  6. protein homotetramerization Source: Ensembl
  7. pyruvate biosynthetic process Source: Ensembl
  8. response to drug Source: RGD
  9. response to lipopolysaccharide Source: Ensembl
  10. response to morphine Source: RGD
  11. response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi5.1.1.18. 5301.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Srr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi735094. Srr.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: RGD
  2. cytoplasm Source: RGD
  3. neuronal cell body Source: Ensembl
  4. plasma membrane Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Serine racemase
PRO_0000286173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561N6-(pyridoxal phosphate)lysine
Modified residuei113 – 1131S-nitrosocysteine By similarity

Post-translational modificationi

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

Keywords - PTMi

S-nitrosylation

Proteomic databases

PaxDbiQ76EQ0.
PRIDEiQ76EQ0.

PTM databases

PhosphoSiteiQ76EQ0.

Expressioni

Gene expression databases

GenevestigatoriQ76EQ0.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000050774.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1911
Turni20 – 223
Helixi32 – 387
Beta strandi40 – 467
Helixi47 – 493
Helixi51 – 533
Helixi57 – 6610
Beta strandi70 – 734
Beta strandi79 – 824
Helixi86 – 9712
Beta strandi102 – 1076
Helixi112 – 1209
Beta strandi124 – 1285
Helixi134 – 14613
Beta strandi153 – 1553
Helixi157 – 1637
Helixi165 – 1739
Beta strandi179 – 1835
Beta strandi185 – 1873
Helixi188 – 20013
Beta strandi204 – 2118
Helixi212 – 2143
Helixi216 – 2238
Helixi238 – 2403
Turni246 – 2483
Helixi249 – 2557
Beta strandi258 – 2625
Helixi264 – 27815
Helixi284 – 29411
Helixi296 – 3005
Beta strandi307 – 3126

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HMKX-ray2.10A/B1-333[»]
3L6CX-ray2.20A/B1-333[»]
ProteinModelPortaliQ76EQ0.

Miscellaneous databases

EvolutionaryTraceiQ76EQ0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2392Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1171.
GeneTreeiENSGT00550000075026.
HOGENOMiHOG000046974.
HOVERGENiHBG023167.
InParanoidiQ76EQ0.
KOiK12235.
OMAiNIGPNTW.
OrthoDBiEOG7HB5B2.
PhylomeDBiQ76EQ0.
TreeFamiTF313346.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q76EQ0-1 [UniParc]FASTAAdd to Basket

« Hide

MCAQYCISFA DVEKAHLNIQ DSVHLTPVLT SSILNQIAGR NLFFKCELFQ    50
KTGSFKIRGA LNAIRGLIPD TLEGKPKAVV THSSGNHGQA LTYAAKLEGI 100
PAYIVVPQTA PNCKKLAIQA YGASIVYSEP SDESRENVAQ RIIQETEGIL 150
VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGMV AGIAITIKTL 200
KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV KSSIGLNTWP 250
IIRDLVDDVF TVTEDEIKYA TQLVWERMKL LIEPTAGVGL AAVLSQHFQT 300
VSPEVKNICI VLSGGNVDLT SLSWVKQAER PAP 333
Length:333
Mass (Da):35,693
Last modified:July 5, 2004 - v1
Checksum:iB0DDD8B7B5A8116C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB106282 mRNA. Translation: BAC84968.1.
BC082014 mRNA. Translation: AAH82014.1.
RefSeqiNP_942052.1. NM_198757.2.
UniGeneiRn.220332.

Genome annotation databases

EnsembliENSRNOT00000046110; ENSRNOP00000050774; ENSRNOG00000002991.
GeneIDi303306.
KEGGirno:303306.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB106282 mRNA. Translation: BAC84968.1 .
BC082014 mRNA. Translation: AAH82014.1 .
RefSeqi NP_942052.1. NM_198757.2.
UniGenei Rn.220332.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3HMK X-ray 2.10 A/B 1-333 [» ]
3L6C X-ray 2.20 A/B 1-333 [» ]
ProteinModelPortali Q76EQ0.
ModBasei Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000050774.

PTM databases

PhosphoSitei Q76EQ0.

Proteomic databases

PaxDbi Q76EQ0.
PRIDEi Q76EQ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000046110 ; ENSRNOP00000050774 ; ENSRNOG00000002991 .
GeneIDi 303306.
KEGGi rno:303306.

Organism-specific databases

CTDi 63826.
RGDi 735094. Srr.

Phylogenomic databases

eggNOGi COG1171.
GeneTreei ENSGT00550000075026.
HOGENOMi HOG000046974.
HOVERGENi HBG023167.
InParanoidi Q76EQ0.
KOi K12235.
OMAi NIGPNTW.
OrthoDBi EOG7HB5B2.
PhylomeDBi Q76EQ0.
TreeFami TF313346.

Enzyme and pathway databases

BRENDAi 5.1.1.18. 5301.

Miscellaneous databases

EvolutionaryTracei Q76EQ0.
NextBioi 651104.
PROi Q76EQ0.

Gene expression databases

Genevestigatori Q76EQ0.

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiSRR_RAT
AccessioniPrimary (citable) accession number: Q76EQ0
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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