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
Homo sapiens (Human)
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
L-serine = pyruvate + NH3.1 Publication
D-serine = pyruvate + NH3.1 Publication

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. 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: GO_Central
  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: GO_Central
  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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9GZT4.
CleanExiHS_SRR.
ExpressionAtlasiQ9GZT4. baseline and differential.
GenevestigatoriQ9GZT4.

Organism-specific databases

HPAiCAB015343.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi121963. 8 interactions.
STRINGi9606.ENSP00000339435.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000075026.
HOGENOMiHOG000046974.
HOVERGENiHBG023167.
InParanoidiQ9GZT4.
KOiK12235.
OMAiWKEEYLT.
OrthoDBiEOG7HB5B2.
PhylomeDBiQ9GZT4.
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.

Q9GZT4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCAQYCISFA DVEKAHINIR DSIHLTPVLT SSILNQLTGR NLFFKCELFQ
60 70 80 90 100
KTGSFKIRGA LNAVRSLVPD ALERKPKAVV THSSGNHGQA LTYAAKLEGI
110 120 130 140 150
PAYIVVPQTA PDCKKLAIQA YGASIVYCEP SDESRENVAK RVTEETEGIM
160 170 180 190 200
VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGML AGIAITVKAL
210 220 230 240 250
KPSVKVYAAE PSNADDCYQS KLKGKLMPNL YPPETIADGV KSSIGLNTWP
260 270 280 290 300
IIRDLVDDIF TVTEDEIKCA TQLVWERMKL LIEPTAGVGV AAVLSQHFQT
310 320 330 340
VSPEVKNICI VLSGGNVDLT SSITWVKQAE RPASYQSVSV
Length:340
Mass (Da):36,566
Last modified:March 1, 2001 - v1
Checksum:i873342C62D5D7B9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi121963. 8 interactions.
STRINGi9606.ENSP00000339435.

Chemistry

BindingDBiQ9GZT4.
ChEMBLiCHEMBL4460.
DrugBankiDB00133. L-Serine.

PTM databases

PhosphoSiteiQ9GZT4.

Polymorphism databases

DMDMi20139924.

Proteomic databases

MaxQBiQ9GZT4.
PaxDbiQ9GZT4.
PRIDEiQ9GZT4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi63826.
GeneCardsiGC17P002212.
HGNCiHGNC:14398. SRR.
HPAiCAB015343.
MIMi606477. gene.
neXtProtiNX_Q9GZT4.
PharmGKBiPA37877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1171.
GeneTreeiENSGT00550000075026.
HOGENOMiHOG000046974.
HOVERGENiHBG023167.
InParanoidiQ9GZT4.
KOiK12235.
OMAiWKEEYLT.
OrthoDBiEOG7HB5B2.
PhylomeDBiQ9GZT4.
TreeFamiTF313346.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSRR. human.
EvolutionaryTraceiQ9GZT4.
GeneWikiiSerine_racemase.
GenomeRNAii63826.
NextBioi65538.
PROiQ9GZT4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9GZT4.
CleanExiHS_SRR.
ExpressionAtlasiQ9GZT4. baseline and differential.
GenevestigatoriQ9GZT4.

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...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 113 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

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 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.