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Q9GZT4 (SRR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SRR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8

Catalytic activity

L-serine = D-serine. Ref.8

L-serine = pyruvate + NH3. Ref.8

D-serine = pyruvate + NH3. Ref.8

Cofactor

Pyridoxal phosphate. Ref.8

Enzyme regulation

Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP. Competitively inhibited by malonate.

Subunit structure

Homodimer. Ref.8

Tissue specificity

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. Ref.2

Post-translational modification

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

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Biophysicochemical properties

Kinetic parameters:

KM=6.5 mM for L-serine Ref.8

Ontologies

Keywords
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Pyridoxal phosphate
   Molecular functionIsomerase
Lyase
   PTMS-nitrosylation
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processD-serine biosynthetic process

Inferred from direct assay Ref.1Ref.2. Source: UniProtKB

D-serine metabolic process

Inferred from direct assay Ref.8. Source: UniProtKB

L-serine metabolic process

Inferred from direct assay Ref.1Ref.2Ref.8. Source: UniProtKB

aging

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

pyruvate biosynthetic process

Inferred from direct assay PubMed 18812225. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from expression pattern PubMed 15681805. Source: UniProtKB

response to morphine

Inferred from electronic annotation. Source: Ensembl

serine family amino acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentapical part of cell

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 16314870. Source: UniProtKB

neuronal cell body

Inferred from direct assay PubMed 17880399. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay Ref.8. Source: UniProtKB

D-serine ammonia-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

L-serine ammonia-lyase activity

Inferred from direct assay PubMed 18812225. Source: UniProtKB

PDZ domain binding

Inferred from physical interaction PubMed 16314870. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

glycine binding

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.8. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 15681805. Source: UniProtKB

pyridoxal phosphate binding

Inferred from direct assay Ref.8. Source: UniProtKB

serine racemase activity

Inferred from direct assay Ref.1Ref.2Ref.8. Source: UniProtKB

threonine racemase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Serine racemase
PRO_0000185650

Regions

Region238 – 2392Substrate binding By similarity

Sites

Active site561Proton acceptor By similarity
Active site841Proton acceptor By similarity
Metal binding2101Magnesium
Metal binding2141Magnesium; via carbonyl oxygen
Metal binding2161Magnesium
Binding site511ATP By similarity
Binding site1211ATP By similarity
Binding site1351Substrate Probable

Amino acid modifications

Modified residue561N6-(pyridoxal phosphate)lysine
Modified residue1131S-nitrosocysteine By similarity

Secondary structure

....................................................... 340
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9GZT4 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 873342C62D5D7B9D

FASTA34036,566
        10         20         30         40         50         60 
MCAQYCISFA DVEKAHINIR DSIHLTPVLT SSILNQLTGR NLFFKCELFQ KTGSFKIRGA 

        70         80         90        100        110        120 
LNAVRSLVPD ALERKPKAVV THSSGNHGQA LTYAAKLEGI PAYIVVPQTA PDCKKLAIQA 

       130        140        150        160        170        180 
YGASIVYCEP SDESRENVAK RVTEETEGIM VHPNQEPAVI AGQGTIALEV LNQVPLVDAL 

       190        200        210        220        230        240 
VVPVGGGGML AGIAITVKAL KPSVKVYAAE PSNADDCYQS KLKGKLMPNL YPPETIADGV 

       250        260        270        280        290        300 
KSSIGLNTWP IIRDLVDDIF TVTEDEIKCA TQLVWERMKL LIEPTAGVGV AAVLSQHFQT 

       310        320        330        340 
VSPEVKNICI VLSGGNVDLT SSITWVKQAE RPASYQSVSV 

« Hide

References

« Hide 'large scale' references
[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]"Characterization and localization of a human serine racemase."
Xia M., Liu Y., Figueroa D.J., Chiu C.S., Wei N., Lawlor A.M., Lu P., Sur C., Koblan K.S., Connolly T.M.
Brain Res. Mol. Brain Res. 125:96-104(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_068766.1. NM_021947.1.
UniGeneHs.461954.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3L6BX-ray1.50A3-340[»]
3L6RX-ray1.70A3-340[»]
ProteinModelPortalQ9GZT4.
SMRQ9GZT4. Positions 3-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121963. 7 interactions.
STRING9606.ENSP00000339435.

Chemistry

BindingDBQ9GZT4.
ChEMBLCHEMBL4460.
DrugBankDB00133. L-Serine.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteQ9GZT4.

Polymorphism databases

DMDM20139924.

Proteomic databases

PaxDbQ9GZT4.
PRIDEQ9GZT4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344595; ENSP00000339435; ENSG00000167720.
GeneID63826.
KEGGhsa:63826.
UCSCuc002fue.1. human.

Organism-specific databases

CTD63826.
GeneCardsGC17P002212.
HGNCHGNC:14398. SRR.
HPACAB015343.
MIM606477. gene.
neXtProtNX_Q9GZT4.
PharmGKBPA37877.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1171.
HOGENOMHOG000046974.
HOVERGENHBG023167.
InParanoidQ9GZT4.
KOK12235.
OMADTPKTIA.
OrthoDBEOG7HB5B2.
PhylomeDBQ9GZT4.
TreeFamTF313346.

Enzyme and pathway databases

BioCycMetaCyc:HS09614-MONOMER.
BRENDA5.1.1.18. 2681.
SignaLinkQ9GZT4.

Gene expression databases

ArrayExpressQ9GZT4.
BgeeQ9GZT4.
CleanExHS_SRR.
GenevestigatorQ9GZT4.

Family and domain databases

InterProIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSRR. human.
EvolutionaryTraceQ9GZT4.
GeneWikiSerine_racemase.
GenomeRNAi63826.
NextBio65538.
PROQ9GZT4.
SOURCESearch...

Entry information

Entry nameSRR_HUMAN
AccessionPrimary (citable) accession number: Q9GZT4
Secondary accession number(s): D3DTI5, Q6IA55
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM