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Protein

Serine racemase

Gene

Srr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.5 Publications

Catalytic activityi

L-serine = D-serine.4 Publications
D-serine = pyruvate + NH3.1 Publication
L-serine = pyruvate + NH3.3 Publications

Cofactori

pyridoxal 5'-phosphate2 Publications

Enzyme regulationi

Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei51ATPCurated1
Active sitei56Proton acceptorBy similarity1
Active sitei84Proton acceptorBy similarity1
Binding sitei121ATPBy similarity1
Binding sitei135SubstrateBy similarity1
Metal bindingi210MagnesiumBy similarity1
Metal bindingi214Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi216MagnesiumBy similarity1

GO - Molecular functioni

  • ATP binding Source: MGI
  • calcium ion binding Source: MGI
  • D-serine ammonia-lyase activity Source: GO_Central
  • glycine binding Source: MGI
  • L-serine ammonia-lyase activity Source: MGI
  • magnesium ion binding Source: MGI
  • PDZ domain binding Source: MGI
  • protein homodimerization activity Source: MGI
  • pyridoxal phosphate binding Source: MGI
  • serine racemase activity Source: MGI
  • threonine racemase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi4.3.1.17. 3474.
5.1.1.18. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine racemase1 Publication (EC:5.1.1.184 Publications)
Alternative name(s):
D-serine ammonia-lyase
D-serine dehydratase (EC:4.3.1.181 Publication)
L-serine ammonia-lyase
L-serine dehydratase (EC:4.3.1.173 Publications)
Gene namesi
Name:Srr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1351636. Srr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi51K → A: Impairs ATP-binding inducing a 80% decrease in enzyme activity. 1
Mutagenesisi113C → S: Abolishes S-nitrosylation. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075306.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001856511 – 339Serine racemaseAdd BLAST339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei56N6-(pyridoxal phosphate)lysineBy similarity1
Modified residuei71PhosphothreonineCombined sources1
Modified residuei113S-nitrosocysteine1 Publication1

Post-translational modificationi

S-nitrosylated, leading to decrease the enzyme activity.1 Publication

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiQ9QZX7.
PeptideAtlasiQ9QZX7.
PRIDEiQ9QZX7.

PTM databases

iPTMnetiQ9QZX7.
PhosphoSitePlusiQ9QZX7.

Expressioni

Tissue specificityi

Detected in brain (at protein level). Brain.

Gene expression databases

BgeeiENSMUSG00000001323.
CleanExiMM_SRR.
ExpressionAtlasiQ9QZX7. baseline and differential.
GenevisibleiQ9QZX7. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • PDZ domain binding Source: MGI
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi205172. 3 interactors.
IntActiQ9QZX7. 2 interactors.
MINTiMINT-5202279.
STRINGi10090.ENSMUSP00000067552.

Chemistry databases

BindingDBiQ9QZX7.

Structurei

3D structure databases

ProteinModelPortaliQ9QZX7.
SMRiQ9QZX7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni238 – 239Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1250. Eukaryota.
COG1171. LUCA.
GeneTreeiENSGT00550000075026.
HOVERGENiHBG023167.
InParanoidiQ9QZX7.
KOiK12235.
OMAiIAYWTQW.
OrthoDBiEOG091G0FSJ.
PhylomeDBiQ9QZX7.
TreeFamiTF313346.

Family and domain databases

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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QZX7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCAQYCISFA DVEKAHINIQ DSIHLTPVLT SSILNQIAGR NLFFKCELFQ
60 70 80 90 100
KTGSFKIRGA LNAIRGLIPD TPEEKPKAVV THSSGNHGQA LTYAAKLEGI
110 120 130 140 150
PAYIVVPQTA PNCKKLAIQA YGASIVYCDP SDESREKVTQ RIMQETEGIL
160 170 180 190 200
VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGMV AGIAITIKAL
210 220 230 240 250
KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV KSSIGLNTWP
260 270 280 290 300
IIRDLVDDVF TVTEDEIKYA TQLVWGRMKL LIEPTAGVAL AAVLSQHFQT
310 320 330
VSPEVKNVCI VLSGGNVDLT SLNWVGQAER PAPYQTVSV
Length:339
Mass (Da):36,359
Last modified:May 1, 2000 - v1
Checksum:iB9AE9A9336358728
GO
Isoform 2 (identifier: Q9QZX7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-198: Missing.

Show »
Length:314
Mass (Da):34,030
Checksum:i0BB6492649FF8491
GO
Isoform 3 (identifier: Q9QZX7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     183-339: Missing.

Note: No experimental confirmation available.
Show »
Length:182
Mass (Da):19,694
Checksum:i23075946C01AF288
GO

Sequence cautioni

The sequence CAI24255 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti111P → T in BAC25712 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_025013174 – 198Missing in isoform 2. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_025014183 – 339Missing in isoform 3. CuratedAdd BLAST157

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148321 mRNA. Translation: AAF08701.1.
AK031687 mRNA. Translation: BAC27514.1.
AK028034 mRNA. Translation: BAC25712.1.
AK043738 mRNA. Translation: BAC31637.1.
AK157122 mRNA. Translation: BAE33968.1.
AK170096 mRNA. Translation: BAE41561.1.
AL604066 Genomic DNA. Translation: CAI24252.1.
AL604066 Genomic DNA. Translation: CAI24253.1.
AL604066 Genomic DNA. Translation: CAI24254.1.
AL604066 Genomic DNA. Translation: CAI24255.1. Sequence problems.
BC011164 mRNA. Translation: AAH11164.1.
AB232340 mRNA. Translation: BAE19920.1.
AB232341 mRNA. Translation: BAE19921.1.
AB232342 mRNA. Translation: BAE19922.1.
AB232343 mRNA. Translation: BAE19923.1.
AB235396 mRNA. Translation: BAE44529.1.
CCDSiCCDS25038.1. [Q9QZX7-1]
RefSeqiNP_001156783.1. NM_001163311.1. [Q9QZX7-1]
NP_038789.1. NM_013761.4. [Q9QZX7-1]
XP_006533520.1. XM_006533457.3. [Q9QZX7-1]
XP_017170058.1. XM_017314569.1. [Q9QZX7-1]
XP_017170059.1. XM_017314570.1. [Q9QZX7-1]
XP_017170060.1. XM_017314571.1. [Q9QZX7-1]
UniGeneiMm.131443.
Mm.220843.
Mm.412219.

Genome annotation databases

EnsembliENSMUST00000065211; ENSMUSP00000067552; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000108447; ENSMUSP00000104086; ENSMUSG00000001323. [Q9QZX7-2]
ENSMUST00000108448; ENSMUSP00000104087; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000121738; ENSMUSP00000113372; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000128556; ENSMUSP00000120012; ENSMUSG00000001323. [Q9QZX7-3]
GeneIDi27364.
KEGGimmu:27364.
UCSCiuc007kcr.2. mouse. [Q9QZX7-1]
uc011xzd.1. mouse. [Q9QZX7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148321 mRNA. Translation: AAF08701.1.
AK031687 mRNA. Translation: BAC27514.1.
AK028034 mRNA. Translation: BAC25712.1.
AK043738 mRNA. Translation: BAC31637.1.
AK157122 mRNA. Translation: BAE33968.1.
AK170096 mRNA. Translation: BAE41561.1.
AL604066 Genomic DNA. Translation: CAI24252.1.
AL604066 Genomic DNA. Translation: CAI24253.1.
AL604066 Genomic DNA. Translation: CAI24254.1.
AL604066 Genomic DNA. Translation: CAI24255.1. Sequence problems.
BC011164 mRNA. Translation: AAH11164.1.
AB232340 mRNA. Translation: BAE19920.1.
AB232341 mRNA. Translation: BAE19921.1.
AB232342 mRNA. Translation: BAE19922.1.
AB232343 mRNA. Translation: BAE19923.1.
AB235396 mRNA. Translation: BAE44529.1.
CCDSiCCDS25038.1. [Q9QZX7-1]
RefSeqiNP_001156783.1. NM_001163311.1. [Q9QZX7-1]
NP_038789.1. NM_013761.4. [Q9QZX7-1]
XP_006533520.1. XM_006533457.3. [Q9QZX7-1]
XP_017170058.1. XM_017314569.1. [Q9QZX7-1]
XP_017170059.1. XM_017314570.1. [Q9QZX7-1]
XP_017170060.1. XM_017314571.1. [Q9QZX7-1]
UniGeneiMm.131443.
Mm.220843.
Mm.412219.

3D structure databases

ProteinModelPortaliQ9QZX7.
SMRiQ9QZX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205172. 3 interactors.
IntActiQ9QZX7. 2 interactors.
MINTiMINT-5202279.
STRINGi10090.ENSMUSP00000067552.

Chemistry databases

BindingDBiQ9QZX7.
ChEMBLiCHEMBL1075306.

PTM databases

iPTMnetiQ9QZX7.
PhosphoSitePlusiQ9QZX7.

Proteomic databases

PaxDbiQ9QZX7.
PeptideAtlasiQ9QZX7.
PRIDEiQ9QZX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065211; ENSMUSP00000067552; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000108447; ENSMUSP00000104086; ENSMUSG00000001323. [Q9QZX7-2]
ENSMUST00000108448; ENSMUSP00000104087; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000121738; ENSMUSP00000113372; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000128556; ENSMUSP00000120012; ENSMUSG00000001323. [Q9QZX7-3]
GeneIDi27364.
KEGGimmu:27364.
UCSCiuc007kcr.2. mouse. [Q9QZX7-1]
uc011xzd.1. mouse. [Q9QZX7-2]

Organism-specific databases

CTDi63826.
MGIiMGI:1351636. Srr.

Phylogenomic databases

eggNOGiKOG1250. Eukaryota.
COG1171. LUCA.
GeneTreeiENSGT00550000075026.
HOVERGENiHBG023167.
InParanoidiQ9QZX7.
KOiK12235.
OMAiIAYWTQW.
OrthoDBiEOG091G0FSJ.
PhylomeDBiQ9QZX7.
TreeFamiTF313346.

Enzyme and pathway databases

BRENDAi4.3.1.17. 3474.
5.1.1.18. 3474.

Miscellaneous databases

PROiQ9QZX7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001323.
CleanExiMM_SRR.
ExpressionAtlasiQ9QZX7. baseline and differential.
GenevisibleiQ9QZX7. MM.

Family and domain databases

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

Entry informationi

Entry nameiSRR_MOUSE
AccessioniPrimary (citable) accession number: Q9QZX7
Secondary accession number(s): Q401M7
, Q5SWE4, Q5SWE5, Q5SWE7, Q8BT19, Q8CD11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 129 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

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.