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Serine racemase (AtSR) (EC 4.3.1.17) (EC 4.3.1.18) (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (L-serine ammonia-lyase) (L-serine dehydratase)

 SRR_ARATH               Reviewed;         331 AA.
Q2PGG3; Q9T0D1;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
07-FEB-2006, sequence version 1.
07-JUN-2017, entry version 83.
RecName: Full=Serine racemase;
Short=AtSR;
EC=4.3.1.17;
EC=4.3.1.18;
EC=5.1.1.18;
AltName: Full=D-serine ammonia-lyase;
AltName: Full=D-serine dehydratase;
AltName: Full=L-serine ammonia-lyase;
AltName: Full=L-serine dehydratase;
Name=SR; Synonyms=SR1; OrderedLocusNames=At4g11640; ORFNames=T5C23.70;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=16483618; DOI=10.1016/j.phytochem.2006.01.003;
Fujitani Y., Nakajima N., Ishihara K., Oikawa T., Ito K., Sugimoto M.;
"Molecular and biochemical characterization of a serine racemase from
Arabidopsis thaliana.";
Phytochemistry 67:668-674(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
DISRUPTION PHENOTYPE.
PubMed=21415319; DOI=10.1126/science.1201101;
Michard E., Lima P.T., Borges F., Silva A.C., Portes M.T.,
Carvalho J.E., Gilliham M., Liu L.H., Obermeyer G., Feijo J.A.;
"Glutamate receptor-like genes form Ca2+ channels in pollen tubes and
are regulated by pistil D-serine.";
Science 332:434-437(2011).
-!- FUNCTION: Catalyzes the synthesis of D-serine from L-serine. Has
dehydratase activity towards both L-serine and D-serine. Displays
high substrate specificity for L-serine, whereas L-alanine, L-
arginine, and L-glutamine were poor substrates.
{ECO:0000269|PubMed:16483618}.
-!- CATALYTIC ACTIVITY: L-serine = D-serine.
-!- CATALYTIC ACTIVITY: L-serine = pyruvate + NH(3).
-!- CATALYTIC ACTIVITY: D-serine = pyruvate + NH(3).
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- ENZYME REGULATION: Inhibited by hydroxylamine. Racemase activity
is enhanced by Ca(2+), Mg(2+), Mn(2+), and is decreased by Ni(2+),
Zn(2+). Hydratase activity is enhanced by Ca(2+), Mg(2+), Mn(2+),
Cu(2+), Fe(2+), Ni(2+). {ECO:0000269|PubMed:16483618}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.5 mM for L-serine (racemase activity)
{ECO:0000269|PubMed:16483618};
KM=0.77 mM for D-serine (racemase activity)
{ECO:0000269|PubMed:16483618};
KM=20 mM for L-serine (dehydratase activity)
{ECO:0000269|PubMed:16483618};
KM=5 mM for D-serine (dehydratase activity)
{ECO:0000269|PubMed:16483618};
Vmax=5 nmol/min/mg enzyme toward L-serine (racemase activity)
{ECO:0000269|PubMed:16483618};
Vmax=1.1 nmol/min/mg enzyme toward D-serine (racemase activity)
{ECO:0000269|PubMed:16483618};
Vmax=250 nmol/min/mg enzyme toward L-serine (dehydratase
activity) {ECO:0000269|PubMed:16483618};
Vmax=26 nmol/min/mg enzyme toward L-serine (dehydratase
activity) {ECO:0000269|PubMed:16483618};
pH dependence:
Optimum pH is 8.5 for racemization and 9.5 for dehydration.
{ECO:0000269|PubMed:16483618};
-!- SUBUNIT: Homodimer. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the whole plant.
{ECO:0000269|PubMed:16483618}.
-!- DISRUPTION PHENOTYPE: Deformations and branching of pollen tubes
grown in pistils. {ECO:0000269|PubMed:21415319}.
-!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB39935.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB78207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AB206823; BAE72067.1; -; mRNA.
EMBL; AL049500; CAB39935.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161532; CAB78207.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE83032.1; -; Genomic_DNA.
PIR; T04211; T04211.
RefSeq; NP_192901.2; NM_117233.3.
UniGene; At.33551; -.
ProteinModelPortal; Q2PGG3; -.
SMR; Q2PGG3; -.
STRING; 3702.AT4G11640.1; -.
PaxDb; Q2PGG3; -.
EnsemblPlants; AT4G11640.1; AT4G11640.1; AT4G11640.
GeneID; 826769; -.
Gramene; AT4G11640.1; AT4G11640.1; AT4G11640.
KEGG; ath:AT4G11640; -.
Araport; AT4G11640; -.
TAIR; locus:2139767; AT4G11640.
eggNOG; KOG1251; Eukaryota.
eggNOG; COG1171; LUCA.
HOGENOM; HOG000046974; -.
InParanoid; Q2PGG3; -.
KO; K12235; -.
OMA; LIHPFDH; -.
OrthoDB; EOG09360GVY; -.
PhylomeDB; Q2PGG3; -.
BioCyc; ARA:AT4G11640-MONOMER; -.
BioCyc; MetaCyc:MONOMER-14684; -.
BRENDA; 5.1.1.18; 399.
PRO; PR:Q2PGG3; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; Q2PGG3; AT.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008721; F:D-serine ammonia-lyase activity; IDA:UniProtKB.
GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043621; F:protein self-association; IEA:EnsemblPlants.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0030378; F:serine racemase activity; IDA:TAIR.
GO; GO:0070178; P:D-serine metabolic process; IDA:UniProtKB.
GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
GO; GO:0009069; P:serine family amino acid metabolic process; IDA:TAIR.
InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
InterPro; IPR001926; TrpB-like_PLP-dep.
Pfam; PF00291; PALP; 1.
SUPFAM; SSF53686; SSF53686; 1.
PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
1: Evidence at protein level;
Allosteric enzyme; ATP-binding; Complete proteome; Isomerase; Lyase;
Magnesium; Metal-binding; Nucleotide-binding; Pyridoxal phosphate;
Reference proteome.
CHAIN 1 331 Serine racemase.
/FTId=PRO_0000420346.
REGION 237 238 Substrate binding. {ECO:0000250}.
ACT_SITE 59 59 Proton acceptor. {ECO:0000250}.
ACT_SITE 84 84 Proton acceptor. {ECO:0000250}.
METAL 210 210 Magnesium. {ECO:0000250}.
METAL 214 214 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 216 216 Magnesium. {ECO:0000250}.
BINDING 54 54 ATP. {ECO:0000250}.
BINDING 121 121 ATP. {ECO:0000250}.
BINDING 135 135 Substrate. {ECO:0000250}.
MOD_RES 59 59 N6-(pyridoxal phosphate)lysine.
{ECO:0000250}.
SEQUENCE 331 AA; 35068 MW; F4FC4EE39DD60A7A CRC64;
MEANREKYAA DILSIKEAHD RIKPYIHRTP VLTSESLNSI SGRSLFFKCE CLQKGGAFKF
RGACNAVLSL DAEQAAKGVV THSSGNHAAA LSLAAKIQGI PAYIVVPKGA PKCKVDNVIR
YGGKVIWSEA TMSSREEIAS KVLQETGSVL IHPYNDGRII SGQGTIALEL LEQIQEIDAI
VVPISGGGLI SGVALAAKSI KPSIRIIAAE PKGADDAAQS KVAGKIITLP VTNTIADGLR
ASLGDLTWPV VRDLVDDVVT LEECEIIEAM KMCYEILKVS VEPSGAIGLA AVLSNSFRNN
PSCRDCKNIG IVLSGGNVDL GSLWDSFKSS K


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