GLYM2_ARATH
ID GLYM2_ARATH Reviewed; 517 AA.
AC Q94C74; C0Z258; Q8GRI1;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Serine hydroxymethyltransferase 2, mitochondrial {ECO:0000303|PubMed:10806255};
DE Short=AtSHMT2 {ECO:0000303|PubMed:31873125};
DE EC=2.1.2.1 {ECO:0000269|PubMed:31873125};
DE AltName: Full=Glycine hydroxymethyltransferase 2 {ECO:0000305};
DE AltName: Full=Serine methylase 2 {ECO:0000305};
DE Flags: Precursor;
GN Name=SHM2 {ECO:0000303|PubMed:10806255};
GN Synonyms=SHMT2 {ECO:0000303|PubMed:31873125};
GN OrderedLocusNames=At5g26780 {ECO:0000312|Araport:AT5G26780};
GN ORFNames=F2P16.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=10806255; DOI=10.1104/pp.123.1.381;
RA McClung C.R., Hsu M., Painter J.E., Gagne J.M., Karlsberg S.D.,
RA Salome P.A.;
RT "Integrated temporal regulation of the photorespiratory pathway. Circadian
RT regulation of two Arabidopsis genes encoding serine
RT hydroxymethyltransferase.";
RL Plant Physiol. 123:381-392(2000).
RN [6]
RP REVIEW.
RX PubMed=12730263; DOI=10.1093/jxb/erg171;
RA Bauwe H., Kolukisaoglu U.;
RT "Genetic manipulation of glycine decarboxylation.";
RL J. Exp. Bot. 54:1523-1535(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16339799; DOI=10.1104/pp.105.071399;
RA Voll L.M., Jamai A., Renne P., Voll H., McClung C.R., Weber A.P.;
RT "The photorespiratory Arabidopsis shm1 mutant is deficient in SHM1.";
RL Plant Physiol. 140:59-66(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [10]
RP GENE FAMILY.
RX PubMed=20518745; DOI=10.1042/bj20100566;
RA Zhang Y., Sun K., Sandoval F.J., Santiago K., Roje S.;
RT "One-carbon metabolism in plants: characterization of a plastid serine
RT hydroxymethyltransferase.";
RL Biochem. J. 430:97-105(2010).
RN [11]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=21976482; DOI=10.1104/pp.111.184564;
RA Engel N., Ewald R., Gupta K.J., Zrenner R., Hagemann M., Bauwe H.;
RT "The presequence of Arabidopsis serine hydroxymethyltransferase SHM2
RT selectively prevents import into mesophyll mitochondria.";
RL Plant Physiol. 157:1711-1720(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 54-517 IN COMPLEX WITH SERINE AND
RP THE ANTIFOLATES METHOTREXATE AND PEMETREXED, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=31873125; DOI=10.1038/s41598-019-56043-4;
RA Ruszkowski M., Sekula B., Ruszkowska A., Contestabile R., Nogues I.,
RA Angelaccio S., Szczepaniak A., Dauter Z.;
RT "Structural basis of methotrexate and pemetrexed action on serine
RT hydroxymethyltransferases revealed using plant models.";
RL Sci. Rep. 9:19614-19614(2019).
CC -!- FUNCTION: Functions outside the photorespiratory pathway in catalyzing
CC the interconversion of serine and glycine with the conversion of
CC tetrahydrofolate (THF) into 5,10-methylene-THF.
CC {ECO:0000269|PubMed:16339799, ECO:0000269|PubMed:21976482,
CC ECO:0000269|PubMed:31873125}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O =
CC (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1;
CC Evidence={ECO:0000269|PubMed:31873125};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:31873125};
CC -!- ACTIVITY REGULATION: Inhibited by the antifolate drugs methotrexate and
CC pemetrexed. {ECO:0000269|PubMed:31873125}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.65 mM for L-serine (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=8.05 mM for L-serine (at pH 7.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=2.86 mM for L-serine (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=1.78 mM for L-serine (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=0.71 mM for L-serine (at pH 9.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=83.6 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=153.6 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 7.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=143.9 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=196.1 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=192.4 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 9.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:31873125}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q94C74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94C74-2; Sequence=VSP_046514;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mainly expressed in the shoot apical
CC meristem and roots. Also detected in the leaf vasculature, especially
CC in the protoxylem and adjacent cell layers.
CC {ECO:0000269|PubMed:16339799, ECO:0000269|PubMed:21976482}.
CC -!- DISRUPTION PHENOTYPE: Does not display a lethal photorespiratory
CC phenotype when grown at ambient carbon dioxide.
CC {ECO:0000269|PubMed:16339799}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; AF007270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93602.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93603.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93604.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69726.1; -; Genomic_DNA.
DR EMBL; AY035117; AAK59622.1; -; mRNA.
DR EMBL; BT001097; AAN61005.1; -; mRNA.
DR EMBL; BT001113; AAN64177.1; -; mRNA.
DR EMBL; AK318672; BAH56787.1; -; mRNA.
DR RefSeq; NP_001331385.1; NM_001343982.1. [Q94C74-1]
DR RefSeq; NP_568488.2; NM_122560.2. [Q94C74-2]
DR RefSeq; NP_851080.1; NM_180749.4. [Q94C74-1]
DR RefSeq; NP_851081.1; NM_180750.2. [Q94C74-2]
DR PDB; 6SMN; X-ray; 1.63 A; A/B/C/D=41-517.
DR PDB; 6SMW; X-ray; 1.54 A; A/B/C/D=41-517.
DR PDBsum; 6SMN; -.
DR PDBsum; 6SMW; -.
DR AlphaFoldDB; Q94C74; -.
DR SMR; Q94C74; -.
DR BioGRID; 18011; 8.
DR STRING; 3702.AT5G26780.3; -.
DR PaxDb; Q94C74; -.
DR PRIDE; Q94C74; -.
DR ProteomicsDB; 248433; -. [Q94C74-1]
DR EnsemblPlants; AT5G26780.1; AT5G26780.1; AT5G26780. [Q94C74-1]
DR EnsemblPlants; AT5G26780.2; AT5G26780.2; AT5G26780. [Q94C74-2]
DR EnsemblPlants; AT5G26780.3; AT5G26780.3; AT5G26780. [Q94C74-2]
DR EnsemblPlants; AT5G26780.4; AT5G26780.4; AT5G26780. [Q94C74-1]
DR GeneID; 832736; -.
DR Gramene; AT5G26780.1; AT5G26780.1; AT5G26780. [Q94C74-1]
DR Gramene; AT5G26780.2; AT5G26780.2; AT5G26780. [Q94C74-2]
DR Gramene; AT5G26780.3; AT5G26780.3; AT5G26780. [Q94C74-2]
DR Gramene; AT5G26780.4; AT5G26780.4; AT5G26780. [Q94C74-1]
DR KEGG; ath:AT5G26780; -.
DR Araport; AT5G26780; -.
DR TAIR; locus:2148463; AT5G26780.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_1_1; -.
DR InParanoid; Q94C74; -.
DR OMA; CATTHKV; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; Q94C74; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:Q94C74; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94C74; baseline and differential.
DR Genevisible; Q94C74; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0046655; P:folic acid metabolic process; IBA:GO_Central.
DR GO; GO:0019264; P:glycine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0006544; P:glycine metabolic process; IDA:UniProtKB.
DR GO; GO:0006565; P:L-serine catabolic process; IBA:GO_Central.
DR GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
DR GO; GO:0006730; P:one-carbon metabolic process; IBA:GO_Central.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IBA:GO_Central.
DR CDD; cd00378; SHMT; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00051; SHMT; 1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR001085; Ser_HO-MeTrfase.
DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR InterPro; IPR039429; SHMT-like_dom.
DR PANTHER; PTHR11680; PTHR11680; 1.
DR Pfam; PF00464; SHMT; 1.
DR PIRSF; PIRSF000412; SHMT; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00096; SHMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Mitochondrion; One-carbon metabolism;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..517
FT /note="Serine hydroxymethyltransferase 2, mitochondrial"
FT /id="PRO_0000422347"
FT BINDING 82
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 82
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 102
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 104
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 104
FT /ligand="methotrexate"
FT /ligand_id="ChEBI:CHEBI:50681"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN"
FT BINDING 104
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 112
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 112
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 148..150
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 177
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN"
FT BINDING 184..186
FT /ligand="methotrexate"
FT /ligand_id="ChEBI:CHEBI:50681"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN"
FT BINDING 232
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 260
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 260
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 286
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMW"
FT BINDING 331
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 414
FT /ligand="methotrexate"
FT /ligand_id="ChEBI:CHEBI:50681"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 430
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT BINDING 430
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMN, ECO:0007744|PDB:6SMW"
FT MOD_RES 286
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 368
FT /note="E -> ELDIRPTVIISYGLSMQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_046514"
FT CONFLICT 430
FT /note="R -> H (in Ref. 3; AAK59622)"
FT /evidence="ECO:0000305"
FT HELIX 44..52
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 116..132
FT /evidence="ECO:0007829|PDB:6SMW"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6SMW"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 317..324
FT /evidence="ECO:0007829|PDB:6SMW"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 334..346
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 350..372
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 398..407
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 443..466
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 483..501
FT /evidence="ECO:0007829|PDB:6SMW"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:6SMW"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:6SMW"
SQ SEQUENCE 517 AA; 57342 MW; DB31BC2D18334E31 CRC64;
MALALRRLSS SVKKPISLLS SNGGSLRFMS SLSTAAMAES EKSRSSWIKQ LNASLDEIDP
EVADIIELEK ARQWKGFELI PSENFTSLSV MQAVGSVMTN KYSEGYPGAR YYGGNEYIDM
AETLCQKRAL EAFQLDPSKW GVNVQSLSGS PANFQVYTAL LKPHERIMAL DLPHGGHLSH
GYQTDTKKIS AVSIFFETMP YRLDENTGYI DYDQLEKSAV LFRPKLIVAG ASAYARLYDY
ARIRKVCNKQ KAVMLADMAH ISGLVAAGVI PSPFEYADVV TTTTHKSLRG PRGAMIFFRK
GLKEINKQGK EVMYDYEDRI NQAVFPGLQG GPHNHTITGL AVALKQARTP EYKAYQDQVL
RNCSKFAETL LAKGYDLVSG GTDNHLVLVN LKNKGIDGSR VEKVLELVHI AANKNTVPGD
VSAMVPGGIR MGTPALTSRG FIEEDFAKVA EYFDLAVKIA LKIKAESQGT KLKDFVATMQ
SNEKLQSEMS KLREMVEEYA KQFPTIGFEK ETMRYKE
