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Protein

Serine racemase

Gene

SRR

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

L-serine = D-serine.
L-serine = pyruvate + NH3.
D-serine = pyruvate + NH3.

Cofactori

Enzyme regulationi

Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei51ATPBy similarity1
Active sitei56Proton acceptorBy similarity1
Active sitei84Proton acceptorBy similarity1
Binding sitei121ATPBy similarity1
Binding sitei135SubstrateBy similarity1
Metal bindingi210MagnesiumBy similarity1
Metal bindingi214Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi216MagnesiumBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

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

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 19

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002861721 – 334Serine racemaseAdd BLAST334

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei56N6-(pyridoxal phosphate)lysineBy similarity1
Modified residuei113S-nitrosocysteineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

S-nitrosylation

Proteomic databases

PaxDbiA0JNI4.
PRIDEiA0JNI4.

Expressioni

Gene expression databases

BgeeiENSBTAG00000004223.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005532.

Structurei

3D structure databases

ProteinModelPortaliA0JNI4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni238 – 239Substrate bindingBy similarity2

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1250. Eukaryota.
COG1171. LUCA.
GeneTreeiENSGT00550000075026.
HOGENOMiHOG000046974.
HOVERGENiHBG023167.
InParanoidiA0JNI4.
KOiK12235.
OMAiPEAFDDH.
OrthoDBiEOG091G0FSJ.
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.

A0JNI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDQYCISFA DVEKAHINIR DFIHLTPVLT SSILNQITGR NLFFKCELFQ
60 70 80 90 100
KTGSFKIRGA LNAIRGLISA HPEEKPRAVV AHSSGNHGQA LSFAARLEGI
110 120 130 140 150
PAYVIVPETA PNCKKLAIQA YGASIVYSEQ SEESRENITK RIAEETEGIM
160 170 180 190 200
VHPNQEPAVI AGQGTIAMEV LNQVPLVDAL VVPVGGGGML AGIAVTVKAL
210 220 230 240 250
RPSVKVYAAE PLNADDCYQS KLKGELTPNP YPPETIADGI KSSIGLNTWP
260 270 280 290 300
IIRDLVDDVF TVTEDEIKYA TQLVWERMKL LIEPTAGVGV AVVLSQHFRT
310 320 330
VPAEVKNICI VLSGGNVDLT SLTWVKKQDE KAAP
Length:334
Mass (Da):36,181
Last modified:December 12, 2006 - v1
Checksum:i63277FE33D8FA45F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC126700 mRNA. Translation: AAI26701.1.
RefSeqiNP_001071433.1. NM_001077965.2.
XP_010814138.1. XM_010815836.2.
XP_010814140.1. XM_010815838.2.
UniGeneiBt.102336.

Genome annotation databases

EnsembliENSBTAT00000005532; ENSBTAP00000005532; ENSBTAG00000004223.
GeneIDi525340.
KEGGibta:525340.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC126700 mRNA. Translation: AAI26701.1.
RefSeqiNP_001071433.1. NM_001077965.2.
XP_010814138.1. XM_010815836.2.
XP_010814140.1. XM_010815838.2.
UniGeneiBt.102336.

3D structure databases

ProteinModelPortaliA0JNI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000005532.

Proteomic databases

PaxDbiA0JNI4.
PRIDEiA0JNI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005532; ENSBTAP00000005532; ENSBTAG00000004223.
GeneIDi525340.
KEGGibta:525340.

Organism-specific databases

CTDi63826.

Phylogenomic databases

eggNOGiKOG1250. Eukaryota.
COG1171. LUCA.
GeneTreeiENSGT00550000075026.
HOGENOMiHOG000046974.
HOVERGENiHBG023167.
InParanoidiA0JNI4.
KOiK12235.
OMAiPEAFDDH.
OrthoDBiEOG091G0FSJ.
TreeFamiTF313346.

Gene expression databases

BgeeiENSBTAG00000004223.

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...

Entry informationi

Entry nameiSRR_BOVIN
AccessioniPrimary (citable) accession number: A0JNI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 12, 2006
Last modified: September 7, 2016
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

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.