GLYC4_ARATH
ID GLYC4_ARATH Reviewed; 471 AA.
AC O23254; Q8LBY1; Q9FPJ3;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Serine hydroxymethyltransferase 4 {ECO:0000303|PubMed:10806255};
DE Short=AtSHMT4 {ECO:0000303|PubMed:31873125};
DE EC=2.1.2.1 {ECO:0000269|PubMed:31873125};
DE AltName: Full=Glycine hydroxymethyltransferase 4 {ECO:0000305};
DE AltName: Full=Serine methylase 4 {ECO:0000305};
GN Name=SHM4 {ECO:0000303|PubMed:10806255};
GN Synonyms=SHMT4 {ECO:0000303|PubMed:31873125};
GN OrderedLocusNames=At4g13930 {ECO:0000312|Araport:AT4G13930};
GN ORFNames=dl3005c {ECO:0000312|EMBL:CAB10172.1},
GN FCAALL.160 {ECO:0000312|EMBL:CAB78435.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, NOMENCLATURE, INDUCTION, AND TISSUE SPECIFICITY.
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 [7]
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 [8]
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 [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP INTERACTION WITH UBP16.
RX PubMed=23232097; DOI=10.1105/tpc.112.106393;
RA Zhou H., Zhao J., Yang Y., Chen C., Liu Y., Jin X., Chen L., Li X.,
RA Deng X.W., Schumaker K.S., Guo Y.;
RT "Ubiquitin-specific protease16 modulates salt tolerance in Arabidopsis by
RT regulating Na(+)/H(+) antiport activity and serine hydroxymethyltransferase
RT stability.";
RL Plant Cell 24:5106-5122(2012).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH THE ANTIFOLATES
RP METHOTREXATE AND PEMETREXED, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP 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: Catalyzes the interconversion of serine and glycine with the
CC conversion of tetrahydrofolate (THF) into 5,10-methylene-THF.
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=2.56 mM for L-serine (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=0.54 mM for L-serine (at pH 7.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=0.30 mM for L-serine (at pH 8.0 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=0.24 mM for L-serine (at pH 8.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=0.20 mM for L-serine (at pH 9.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:31873125};
CC KM=7.87 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 6.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=14.97 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 7.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=23.83 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.0 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=33.75 uM for (6S)-5,6,7,8-tetrahydrofolate (at pH 8.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:31873125};
CC KM=49.24 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 (PubMed:31873125). Interacts with UBP16
CC (PubMed:23232097). {ECO:0000269|PubMed:23232097,
CC ECO:0000269|PubMed:31873125}.
CC -!- INTERACTION:
CC O23254; Q9SB51: UBP16; NbExp=3; IntAct=EBI-6589432, EBI-6589403;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, less abundant in
CC roots, inflorescence stems, and siliques, and barely detectable in
CC leaves. {ECO:0000269|PubMed:10806255}.
CC -!- INDUCTION: Circadian-regulation. {ECO:0000269|PubMed:10806255}.
CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}.
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DR EMBL; Z97335; CAB10172.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78435.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83344.1; -; Genomic_DNA.
DR EMBL; AF324991; AAG40343.1; -; mRNA.
DR EMBL; AF361589; AAK32757.1; -; mRNA.
DR EMBL; AY093987; AAM16248.1; -; mRNA.
DR EMBL; AY086929; AAM64493.1; -; mRNA.
DR PIR; B71400; B71400.
DR RefSeq; NP_193129.1; NM_117467.4.
DR PDB; 6SMR; X-ray; 2.12 A; A/B/C/D=1-471.
DR PDBsum; 6SMR; -.
DR AlphaFoldDB; O23254; -.
DR SMR; O23254; -.
DR BioGRID; 12324; 5.
DR IntAct; O23254; 3.
DR STRING; 3702.AT4G13930.1; -.
DR iPTMnet; O23254; -.
DR MetOSite; O23254; -.
DR PaxDb; O23254; -.
DR PRIDE; O23254; -.
DR ProMEX; O23254; -.
DR ProteomicsDB; 248430; -.
DR EnsemblPlants; AT4G13930.1; AT4G13930.1; AT4G13930.
DR GeneID; 827027; -.
DR Gramene; AT4G13930.1; AT4G13930.1; AT4G13930.
DR KEGG; ath:AT4G13930; -.
DR Araport; AT4G13930; -.
DR TAIR; locus:2129251; AT4G13930.
DR eggNOG; KOG2467; Eukaryota.
DR HOGENOM; CLU_022477_0_0_1; -.
DR InParanoid; O23254; -.
DR OMA; VTNRNAI; -.
DR OrthoDB; 372408at2759; -.
DR PhylomeDB; O23254; -.
DR BioCyc; ARA:AT4G13930-MON; -.
DR UniPathway; UPA00193; -.
DR PRO; PR:O23254; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O23254; baseline and differential.
DR Genevisible; O23254; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:1901149; F:salicylic acid binding; HDA:TAIR.
DR GO; GO:0070905; F:serine binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
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:0006565; P:L-serine catabolic process; IBA:GO_Central.
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; Acetylation; Cytoplasm; One-carbon metabolism;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..471
FT /note="Serine hydroxymethyltransferase 4"
FT /id="PRO_0000422349"
FT BINDING 39
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:Q94C74"
FT BINDING 39
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 59
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 61
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:Q94C74"
FT BINDING 61
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 69
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:Q94C74"
FT BINDING 105..107
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 134
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 190
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 218
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:Q94C74"
FT BINDING 218
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 244
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:Q94C74"
FT BINDING 290
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 373
FT /ligand="methotrexate"
FT /ligand_id="ChEBI:CHEBI:50681"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT BINDING 389
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:Q94C74"
FT BINDING 389
FT /ligand="pemetrexed"
FT /ligand_id="ChEBI:CHEBI:63724"
FT /evidence="ECO:0000269|PubMed:31873125,
FT ECO:0007744|PDB:6SMR"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 244
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 53
FT /note="S -> R (in Ref. 4; AAG40343)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="S -> P (in Ref. 4; AAG40343)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="I -> T (in Ref. 5; AAM64493)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="K -> Q (in Ref. 5; AAM64493)"
FT /evidence="ECO:0000305"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:6SMR"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:6SMR"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:6SMR"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 309..331
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 342..349
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 357..366
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 393..397
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 402..426
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 441..455
FT /evidence="ECO:0007829|PDB:6SMR"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:6SMR"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:6SMR"
SQ SEQUENCE 471 AA; 51718 MW; 5F5D997042CBD425 CRC64;
MEPVSSWGNT SLVSVDPEIH DLIEKEKRRQ CRGIELIASE NFTSFAVIEA LGSALTNKYS
EGIPGNRYYG GNEFIDEIEN LCRSRALEAF HCDPAAWGVN VQPYSGSPAN FAAYTALLQP
HDRIMGLDLP SGGHLTHGYY TSGGKKISAT SIYFESLPYK VNFTTGYIDY DKLEEKALDF
RPKLLICGGS AYPRDWDYAR FRAIADKVGA LLLCDMAHIS GLVAAQEAAN PFEYCDVVTT
TTHKSLRGPR AGMIFYRKGP KPPKKGQPEG AVYDFEDKIN FAVFPALQGG PHNHQIGALA
VALKQANTPG FKVYAKQVKA NAVALGNYLM SKGYQIVTNG TENHLVLWDL RPLGLTGNKV
EKLCDLCSIT LNKNAVFGDS SALAPGGVRI GAPAMTSRGL VEKDFEQIGE FLSRAVTLTL
DIQKTYGKLL KDFNKGLVNN KDLDQLKADV EKFSASYEMP GFLMSEMKYK D
