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Q9GZT4

- SRR_HUMAN

UniProt

Q9GZT4 - SRR_HUMAN

Protein

Serine racemase

Gene

SRR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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. Competitively inhibited by malonate.

    Kineticsi

    1. KM=6.5 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 – 2101Magnesium
    Metal bindingi214 – 2141Magnesium; via carbonyl oxygen
    Metal bindingi216 – 2161Magnesium

    GO - Molecular functioni

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

    GO - Biological processi

    1. aging Source: Ensembl
    2. brain development Source: Ensembl
    3. D-serine biosynthetic process Source: UniProtKB
    4. D-serine metabolic process Source: UniProtKB
    5. L-serine metabolic process Source: UniProtKB
    6. protein homotetramerization Source: UniProtKB
    7. pyruvate biosynthetic process Source: UniProtKB
    8. response to drug Source: Ensembl
    9. response to lipopolysaccharide Source: UniProtKB
    10. response to morphine Source: Ensembl
    11. serine family amino acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09614-MONOMER.
    BRENDAi5.1.1.18. 2681.
    SignaLinkiQ9GZT4.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:14398. SRR.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. neuronal cell body Source: UniProtKB
    4. plasma membrane Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37877.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 340340Serine racemasePRO_0000185650Add
    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

    MaxQBiQ9GZT4.
    PaxDbiQ9GZT4.
    PRIDEiQ9GZT4.

    PTM databases

    PhosphoSiteiQ9GZT4.

    Expressioni

    Tissue specificityi

    Brain: expressed at high levels in hippocampus and corpus callosum, intermediate levels in substantia nigra and caudate, and low levels in amygdala, thalamus, and subthalamic nuclei. Expressed in heart, skeletal muscle, kidney and liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9GZT4.
    BgeeiQ9GZT4.
    CleanExiHS_SRR.
    GenevestigatoriQ9GZT4.

    Organism-specific databases

    HPAiCAB015343.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi121963. 7 interactions.
    STRINGi9606.ENSP00000339435.

    Structurei

    Secondary structure

    1
    340
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1911
    Helixi20 – 223
    Helixi32 – 387
    Beta strandi40 – 467
    Helixi47 – 493
    Helixi51 – 533
    Helixi56 – 6510
    Beta strandi79 – 824
    Helixi86 – 9712
    Beta strandi102 – 1076
    Helixi112 – 1209
    Beta strandi124 – 1285
    Helixi132 – 14615
    Beta strandi153 – 1553
    Helixi157 – 17317
    Beta strandi179 – 1835
    Beta strandi185 – 1873
    Helixi188 – 20013
    Beta strandi204 – 2118
    Helixi212 – 2143
    Helixi216 – 2238
    Helixi238 – 2403
    Helixi248 – 2558
    Beta strandi258 – 2625
    Helixi264 – 27815
    Helixi284 – 29411
    Helixi296 – 3005
    Beta strandi307 – 3126
    Helixi321 – 3233

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L6BX-ray1.50A1-340[»]
    3L6RX-ray1.70A1-340[»]
    ProteinModelPortaliQ9GZT4.
    SMRiQ9GZT4. Positions 3-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9GZT4.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1171.
    HOGENOMiHOG000046974.
    HOVERGENiHBG023167.
    InParanoidiQ9GZT4.
    KOiK12235.
    OMAiVEHYEAP.
    OrthoDBiEOG7HB5B2.
    PhylomeDBiQ9GZT4.
    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.

    Q9GZT4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCAQYCISFA DVEKAHINIR DSIHLTPVLT SSILNQLTGR NLFFKCELFQ    50
    KTGSFKIRGA LNAVRSLVPD ALERKPKAVV THSSGNHGQA LTYAAKLEGI 100
    PAYIVVPQTA PDCKKLAIQA YGASIVYCEP SDESRENVAK RVTEETEGIM 150
    VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGML AGIAITVKAL 200
    KPSVKVYAAE PSNADDCYQS KLKGKLMPNL YPPETIADGV KSSIGLNTWP 250
    IIRDLVDDIF TVTEDEIKCA TQLVWERMKL LIEPTAGVGV AAVLSQHFQT 300
    VSPEVKNICI VLSGGNVDLT SSITWVKQAE RPASYQSVSV 340
    Length:340
    Mass (Da):36,566
    Last modified:March 1, 2001 - v1
    Checksum:i873342C62D5D7B9D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169974 mRNA. Translation: AAG27081.1.
    AY034081 mRNA. Translation: AAK58495.1.
    AK023169 mRNA. Translation: BAB14442.1.
    CR457300 mRNA. Translation: CAG33581.1.
    CH471108 Genomic DNA. Translation: EAW90553.1.
    CH471108 Genomic DNA. Translation: EAW90554.1.
    CH471108 Genomic DNA. Translation: EAW90555.1.
    BC074728 mRNA. Translation: AAH74728.1.
    CCDSiCCDS11017.1.
    RefSeqiNP_068766.1. NM_021947.1.
    XP_006721628.1. XM_006721565.1.
    XP_006721629.1. XM_006721566.1.
    UniGeneiHs.461954.

    Genome annotation databases

    EnsembliENST00000344595; ENSP00000339435; ENSG00000167720.
    GeneIDi63826.
    KEGGihsa:63826.
    UCSCiuc002fue.1. human.

    Polymorphism databases

    DMDMi20139924.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169974 mRNA. Translation: AAG27081.1 .
    AY034081 mRNA. Translation: AAK58495.1 .
    AK023169 mRNA. Translation: BAB14442.1 .
    CR457300 mRNA. Translation: CAG33581.1 .
    CH471108 Genomic DNA. Translation: EAW90553.1 .
    CH471108 Genomic DNA. Translation: EAW90554.1 .
    CH471108 Genomic DNA. Translation: EAW90555.1 .
    BC074728 mRNA. Translation: AAH74728.1 .
    CCDSi CCDS11017.1.
    RefSeqi NP_068766.1. NM_021947.1.
    XP_006721628.1. XM_006721565.1.
    XP_006721629.1. XM_006721566.1.
    UniGenei Hs.461954.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L6B X-ray 1.50 A 1-340 [» ]
    3L6R X-ray 1.70 A 1-340 [» ]
    ProteinModelPortali Q9GZT4.
    SMRi Q9GZT4. Positions 3-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121963. 7 interactions.
    STRINGi 9606.ENSP00000339435.

    Chemistry

    BindingDBi Q9GZT4.
    ChEMBLi CHEMBL4460.
    DrugBanki DB00133. L-Serine.
    DB00114. Pyridoxal Phosphate.

    PTM databases

    PhosphoSitei Q9GZT4.

    Polymorphism databases

    DMDMi 20139924.

    Proteomic databases

    MaxQBi Q9GZT4.
    PaxDbi Q9GZT4.
    PRIDEi Q9GZT4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344595 ; ENSP00000339435 ; ENSG00000167720 .
    GeneIDi 63826.
    KEGGi hsa:63826.
    UCSCi uc002fue.1. human.

    Organism-specific databases

    CTDi 63826.
    GeneCardsi GC17P002212.
    HGNCi HGNC:14398. SRR.
    HPAi CAB015343.
    MIMi 606477. gene.
    neXtProti NX_Q9GZT4.
    PharmGKBi PA37877.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1171.
    HOGENOMi HOG000046974.
    HOVERGENi HBG023167.
    InParanoidi Q9GZT4.
    KOi K12235.
    OMAi VEHYEAP.
    OrthoDBi EOG7HB5B2.
    PhylomeDBi Q9GZT4.
    TreeFami TF313346.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09614-MONOMER.
    BRENDAi 5.1.1.18. 2681.
    SignaLinki Q9GZT4.

    Miscellaneous databases

    ChiTaRSi SRR. human.
    EvolutionaryTracei Q9GZT4.
    GeneWikii Serine_racemase.
    GenomeRNAii 63826.
    NextBioi 65538.
    PROi Q9GZT4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZT4.
    Bgeei Q9GZT4.
    CleanExi HS_SRR.
    Genevestigatori Q9GZT4.

    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. "Human serine racemase: molecular cloning, genomic organization and functional expression."
      De Miranda J., Santoro A., Engelender S., Wolosker H.
      Gene 256:183-188(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain.
    7. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 97-114; 116-135; 206-221 AND 226-241, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    8. "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 (1.5 ANGSTROMS) OF 3-340 IN COMPLEX WITH MANGANESE IONS; MALONATE AND PYRIDOXAL PHOSPHATE, COFACTOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiSRR_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZT4
    Secondary accession number(s): D3DTI5, Q6IA55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 31, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3