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Q76EQ0

- SRR_RAT

UniProt

Q76EQ0 - SRR_RAT

Protein

Serine racemase

Gene

Srr

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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.By similarity1 Publication

    Kineticsi

    1. KM=3.7 mM for L-serine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei51 – 511ATPBy similarity
    Active sitei56 – 561Proton acceptorBy similarity
    Active sitei84 – 841Proton acceptorBy similarity
    Binding sitei121 – 1211ATPBy similarity
    Binding sitei135 – 1351SubstrateCurated
    Metal bindingi210 – 2101MagnesiumBy similarity
    Metal bindingi214 – 2141Magnesium; via carbonyl oxygen
    Metal bindingi216 – 2161MagnesiumBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. calcium ion binding Source: Ensembl
    3. D-serine ammonia-lyase activity Source: UniProtKB-EC
    4. glycine binding Source: Ensembl
    5. L-serine ammonia-lyase activity Source: UniProtKB-EC
    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

    GO - Biological processi

    1. aging Source: RGD
    2. brain development Source: RGD
    3. D-serine biosynthetic process Source: Ensembl
    4. D-serine metabolic process Source: UniProtKB
    5. L-serine metabolic process Source: UniProtKB
    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

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 333333Serine racemasePRO_0000286173Add
    BLAST

    Amino acid modifications

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

    1
    333
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ76EQ0.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni238 – 2392Substrate bindingBy 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...
    MobiDBi 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

    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: October 1, 2014
    This is version 78 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