SRR_RAT
ID SRR_RAT Reviewed; 333 AA.
AC Q76EQ0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Serine racemase;
DE EC=5.1.1.18 {ECO:0000269|PubMed:20106978};
DE AltName: Full=D-serine ammonia-lyase;
DE AltName: Full=D-serine dehydratase;
DE EC=4.3.1.18 {ECO:0000250|UniProtKB:Q9QZX7};
DE AltName: Full=L-serine ammonia-lyase;
DE AltName: Full=L-serine dehydratase;
DE EC=4.3.1.17 {ECO:0000250|UniProtKB:Q9QZX7};
GN Name=Srr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=12946565; DOI=10.1016/s0304-3940(03)00801-2;
RA Konno R.;
RT "Rat cerebral serine racemase: amino acid deletion and truncation at
RT carboxy terminus.";
RL Neurosci. Lett. 349:111-114(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION.
RX PubMed=16713567; DOI=10.1016/j.cell.2006.02.051;
RA Panatier A., Theodosis D.T., Mothet J.P., Touquet B., Pollegioni L.,
RA Poulain D.A., Oliet S.H.;
RT "Glia-derived D-serine controls NMDA receptor activity and synaptic
RT memory.";
RL Cell 125:775-784(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 3-333 IN COMPLEX WITH MANGANESE
RP IONS; MALONATE AND PYRIDOXAL PHOSPHATE, COFACTOR, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND
RP REACTION MECHANISM.
RX PubMed=20106978; DOI=10.1074/jbc.m109.050062;
RA Smith M.A., Mack V., Ebneth A., Moraes I., Felicetti B., Wood M.,
RA Schonfeld D., Mather O., Cesura A., Barker J.;
RT "The structure of mammalian serine racemase: evidence for conformational
RT changes upon inhibitor binding.";
RL J. Biol. Chem. 285:12873-12881(2010).
CC -!- FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D-serine
CC is a key coagonist with glutamate at NMDA receptors. Has dehydratase
CC activity towards both L-serine and D-serine.
CC {ECO:0000269|PubMed:16713567, ECO:0000269|PubMed:20106978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; EC=5.1.1.18;
CC Evidence={ECO:0000269|PubMed:20106978};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC Evidence={ECO:0000250|UniProtKB:Q9QZX7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q9QZX7};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20106978};
CC -!- ACTIVITY REGULATION: Allosterically activated by magnesium, and
CC possibly also other divalent metal cations. Allosterically activated by
CC ATP, ADP or GTP (By similarity). Competitively inhibited by malonate.
CC {ECO:0000250, ECO:0000269|PubMed:20106978}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 mM for L-serine {ECO:0000269|PubMed:20106978};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20106978}.
CC -!- PTM: S-nitrosylated, leading to decrease the enzyme activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; AB106282; BAC84968.1; -; mRNA.
DR EMBL; BC082014; AAH82014.1; -; mRNA.
DR RefSeq; NP_942052.1; NM_198757.2.
DR RefSeq; XP_008766237.1; XM_008768015.2.
DR PDB; 3HMK; X-ray; 2.10 A; A/B=1-333.
DR PDB; 3L6C; X-ray; 2.20 A; A/B=1-333.
DR PDBsum; 3HMK; -.
DR PDBsum; 3L6C; -.
DR AlphaFoldDB; Q76EQ0; -.
DR SMR; Q76EQ0; -.
DR BioGRID; 257487; 2.
DR STRING; 10116.ENSRNOP00000050774; -.
DR iPTMnet; Q76EQ0; -.
DR PhosphoSitePlus; Q76EQ0; -.
DR PaxDb; Q76EQ0; -.
DR PRIDE; Q76EQ0; -.
DR Ensembl; ENSRNOT00000046110; ENSRNOP00000050774; ENSRNOG00000002991.
DR GeneID; 303306; -.
DR KEGG; rno:303306; -.
DR CTD; 63826; -.
DR RGD; 735094; Srr.
DR eggNOG; KOG1251; Eukaryota.
DR GeneTree; ENSGT00550000075026; -.
DR HOGENOM; CLU_021152_4_2_1; -.
DR InParanoid; Q76EQ0; -.
DR OMA; LIHPFDH; -.
DR OrthoDB; 943371at2759; -.
DR PhylomeDB; Q76EQ0; -.
DR TreeFam; TF313346; -.
DR BRENDA; 5.1.1.18; 5301.
DR Reactome; R-RNO-977347; Serine biosynthesis.
DR SABIO-RK; Q76EQ0; -.
DR EvolutionaryTrace; Q76EQ0; -.
DR PRO; PR:Q76EQ0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002991; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; Q76EQ0; baseline and differential.
DR Genevisible; Q76EQ0; RN.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0016594; F:glycine binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0030378; F:serine racemase activity; IDA:UniProtKB.
DR GO; GO:0018114; F:threonine racemase activity; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0070179; P:D-serine biosynthetic process; ISO:RGD.
DR GO; GO:0070178; P:D-serine metabolic process; IDA:UniProtKB.
DR GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
DR GO; GO:0042866; P:pyruvate biosynthetic process; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0009069; P:serine family amino acid metabolic process; ISO:RGD.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Isomerase; Lyase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; S-nitrosylation.
FT CHAIN 1..333
FT /note="Serine racemase"
FT /id="PRO_0000286173"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 84
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000305"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 216
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 238..239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZX7"
FT MOD_RES 113
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZX7"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:3HMK"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3HMK"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 249..255
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:3HMK"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:3HMK"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3HMK"
SQ SEQUENCE 333 AA; 35693 MW; B0DDD8B7B5A8116C CRC64;
MCAQYCISFA DVEKAHLNIQ DSVHLTPVLT SSILNQIAGR NLFFKCELFQ KTGSFKIRGA
LNAIRGLIPD TLEGKPKAVV THSSGNHGQA LTYAAKLEGI PAYIVVPQTA PNCKKLAIQA
YGASIVYSEP SDESRENVAQ RIIQETEGIL VHPNQEPAVI AGQGTIALEV LNQVPLVDAL
VVPVGGGGMV AGIAITIKTL KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV
KSSIGLNTWP IIRDLVDDVF TVTEDEIKYA TQLVWERMKL LIEPTAGVGL AAVLSQHFQT
VSPEVKNICI VLSGGNVDLT SLSWVKQAER PAP
