Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine racemase

Gene

Srr

Organism
Rattus norvegicus (Rat)
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.2 Publications

Catalytic activityi

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

Cofactori

pyridoxal 5'-phosphate1 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.By similarity1 Publication

Kineticsi

  1. KM=3.7 mM for L-serine1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei51ATPBy similarity1
    Active sitei56Proton acceptorBy similarity1
    Active sitei84Proton acceptorBy similarity1
    Binding sitei121ATPBy similarity1
    Binding sitei135SubstrateCurated1
    Metal bindingi210MagnesiumBy similarity1
    Metal bindingi214Magnesium; via carbonyl oxygen1
    Metal bindingi216MagnesiumBy similarity1

    GO - Molecular functioni

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

    GO - Biological processi

    • aging Source: RGD
    • brain development Source: RGD
    • D-serine biosynthetic process Source: GO_Central
    • D-serine metabolic process Source: UniProtKB
    • L-serine metabolic process Source: UniProtKB
    • protein homotetramerization Source: Ensembl
    • pyruvate biosynthetic process Source: Ensembl
    • response to drug Source: RGD
    • response to lipopolysaccharide Source: Ensembl
    • response to morphine Source: RGD
    • 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.
    SABIO-RKQ76EQ0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine racemase (EC:5.1.1.181 Publication)
    Alternative name(s):
    D-serine ammonia-lyase
    D-serine dehydratase (EC:4.3.1.18By similarity)
    L-serine ammonia-lyase
    L-serine dehydratase (EC:4.3.1.17By similarity)
    Gene namesi
    Name:Srr
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 10

    Organism-specific databases

    RGDi735094. Srr.

    Subcellular locationi

    GO - Cellular componenti

    • apical part of cell Source: RGD
    • cytoplasm Source: RGD
    • neuronal cell body Source: GO_Central
    • plasma membrane Source: RGD
    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002861731 – 333Serine racemaseAdd BLAST333

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei56N6-(pyridoxal phosphate)lysine1
    Modified residuei71PhosphothreonineBy similarity1
    Modified residuei113S-nitrosocysteineBy similarity1

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein, S-nitrosylation

    Proteomic databases

    PaxDbiQ76EQ0.
    PRIDEiQ76EQ0.

    PTM databases

    iPTMnetiQ76EQ0.
    PhosphoSitePlusiQ76EQ0.

    Expressioni

    Gene expression databases

    BgeeiENSRNOG00000002991.
    ExpressionAtlasiQ76EQ0. baseline and differential.
    GenevisibleiQ76EQ0. RN.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    GO - Molecular functioni

    • protein homodimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi257487. 1 interactor.
    STRINGi10116.ENSRNOP00000050774.

    Structurei

    Secondary structure

    1333
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi9 – 19Combined sources11
    Turni20 – 22Combined sources3
    Helixi32 – 38Combined sources7
    Beta strandi40 – 46Combined sources7
    Helixi47 – 49Combined sources3
    Helixi51 – 53Combined sources3
    Helixi57 – 66Combined sources10
    Beta strandi70 – 73Combined sources4
    Beta strandi79 – 82Combined sources4
    Helixi86 – 97Combined sources12
    Beta strandi102 – 107Combined sources6
    Helixi112 – 120Combined sources9
    Beta strandi124 – 128Combined sources5
    Helixi134 – 146Combined sources13
    Beta strandi153 – 155Combined sources3
    Helixi157 – 163Combined sources7
    Helixi165 – 173Combined sources9
    Beta strandi179 – 183Combined sources5
    Beta strandi185 – 187Combined sources3
    Helixi188 – 200Combined sources13
    Beta strandi204 – 211Combined sources8
    Helixi212 – 214Combined sources3
    Helixi216 – 223Combined sources8
    Helixi238 – 240Combined sources3
    Turni246 – 248Combined sources3
    Helixi249 – 255Combined sources7
    Beta strandi258 – 262Combined sources5
    Helixi264 – 278Combined sources15
    Helixi284 – 294Combined sources11
    Helixi296 – 300Combined sources5
    Beta strandi307 – 312Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3HMKX-ray2.10A/B1-333[»]
    3L6CX-ray2.20A/B1-333[»]
    ProteinModelPortaliQ76EQ0.
    SMRiQ76EQ0.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ76EQ0.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1250. Eukaryota.
    COG1171. LUCA.
    GeneTreeiENSGT00550000075026.
    HOGENOMiHOG000046974.
    HOVERGENiHBG023167.
    InParanoidiQ76EQ0.
    KOiK12235.
    OMAiIAYWTQW.
    PhylomeDBiQ76EQ0.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q76EQ0-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MCAQYCISFA DVEKAHLNIQ DSVHLTPVLT SSILNQIAGR NLFFKCELFQ
    60 70 80 90 100
    KTGSFKIRGA LNAIRGLIPD TLEGKPKAVV THSSGNHGQA LTYAAKLEGI
    110 120 130 140 150
    PAYIVVPQTA PNCKKLAIQA YGASIVYSEP SDESRENVAQ RIIQETEGIL
    160 170 180 190 200
    VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGMV AGIAITIKTL
    210 220 230 240 250
    KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV KSSIGLNTWP
    260 270 280 290 300
    IIRDLVDDVF TVTEDEIKYA TQLVWERMKL LIEPTAGVGL AAVLSQHFQT
    310 320 330
    VSPEVKNICI VLSGGNVDLT SLSWVKQAER PAP
    Length:333
    Mass (Da):35,693
    Last modified:July 5, 2004 - v1
    Checksum:iB0DDD8B7B5A8116C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB106282 mRNA. Translation: BAC84968.1.
    BC082014 mRNA. Translation: AAH82014.1.
    RefSeqiNP_942052.1. NM_198757.2.
    XP_008766237.1. XM_008768015.2.
    UniGeneiRn.220332.

    Genome annotation databases

    EnsembliENSRNOT00000046110; ENSRNOP00000050774; ENSRNOG00000002991.
    ENSRNOT00000085394; ENSRNOP00000070927; ENSRNOG00000002991.
    GeneIDi303306.
    KEGGirno:303306.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB106282 mRNA. Translation: BAC84968.1.
    BC082014 mRNA. Translation: AAH82014.1.
    RefSeqiNP_942052.1. NM_198757.2.
    XP_008766237.1. XM_008768015.2.
    UniGeneiRn.220332.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3HMKX-ray2.10A/B1-333[»]
    3L6CX-ray2.20A/B1-333[»]
    ProteinModelPortaliQ76EQ0.
    SMRiQ76EQ0.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi257487. 1 interactor.
    STRINGi10116.ENSRNOP00000050774.

    PTM databases

    iPTMnetiQ76EQ0.
    PhosphoSitePlusiQ76EQ0.

    Proteomic databases

    PaxDbiQ76EQ0.
    PRIDEiQ76EQ0.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000046110; ENSRNOP00000050774; ENSRNOG00000002991.
    ENSRNOT00000085394; ENSRNOP00000070927; ENSRNOG00000002991.
    GeneIDi303306.
    KEGGirno:303306.

    Organism-specific databases

    CTDi63826.
    RGDi735094. Srr.

    Phylogenomic databases

    eggNOGiKOG1250. Eukaryota.
    COG1171. LUCA.
    GeneTreeiENSGT00550000075026.
    HOGENOMiHOG000046974.
    HOVERGENiHBG023167.
    InParanoidiQ76EQ0.
    KOiK12235.
    OMAiIAYWTQW.
    PhylomeDBiQ76EQ0.
    TreeFamiTF313346.

    Enzyme and pathway databases

    BRENDAi5.1.1.18. 5301.
    SABIO-RKQ76EQ0.

    Miscellaneous databases

    EvolutionaryTraceiQ76EQ0.
    PROiQ76EQ0.

    Gene expression databases

    BgeeiENSRNOG00000002991.
    ExpressionAtlasiQ76EQ0. baseline and differential.
    GenevisibleiQ76EQ0. RN.

    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_RAT
    AccessioniPrimary (citable) accession number: Q76EQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: July 5, 2004
    Last modified: November 30, 2016
    This is version 95 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

    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.