ID METE1_ARATH Reviewed; 765 AA. AC O50008; Q6KCR2; Q8H162; Q93ZK3; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 02-SEP-2026, entry version 184. DE RecName: Full=5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1; DE EC=2.1.1.14 {ECO:0000269|PubMed:15024005}; DE AltName: Full=Cobalamin-independent methionine synthase 1; DE Short=AtMS1; DE AltName: Full=Vitamin-B12-independent methionine synthase 1; GN Name=MS1; Synonyms=CIMS; OrderedLocusNames=At5g17920; ORFNames=MPI7.9; 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 [MRNA], AND CHARACTERIZATION. RC STRAIN=cv. Columbia; RX PubMed=9636232; DOI=10.1073/pnas.95.13.7805; RA Ravanel S., Gakiere B., Job D., Douce R.; RT "The specific features of methionine biosynthesis and metabolism in RT plants."; RL Proc. Natl. Acad. Sci. U.S.A. 95:7805-7812(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RA Gakiere B., Job D., Douce R., Ravanel S.; RT "Characterization of the cDNA and gene for a cytosolic cobalamin- RT independent methionine synthase in Arabidopsis thaliana."; RL (er) Plant Gene Register PGR99-115(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC STRAIN=cv. Wassilewskija; RX PubMed=15024005; DOI=10.1074/jbc.m313250200; RA Ravanel S., Block M.A., Rippert P., Jabrin S., Curien G., Rebeille F., RA Douce R.; RT "Methionine metabolism in plants: chloroplasts are autonomous for de novo RT methionine synthesis and can import S-adenosylmethionine from the RT cytosol."; RL J. Biol. Chem. 279:22548-22557(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9679202; DOI=10.1093/dnares/5.2.131; RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence RT features of the regions of 1,381,565 bp covered by twenty one physically RT assigned P1 and TAC clones."; RL DNA Res. 5:131-145(1998). RN [5] 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 [6] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] {ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, ECO:0007744|PDB:1U1U, ECO:0007744|PDB:1U22} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEXES WITH RP 5-METHYLTETRAHYDROFOLATE; L-HOMOCYSTEINE; L-METHIONINE AND ZINC IONS, AND RP COFACTOR. RX PubMed=15326182; DOI=10.1074/jbc.c400325200; RA Ferrer J.L., Ravanel S., Robert M., Dumas R.; RT "Crystal structures of cobalamin-independent methionine synthase complexed RT with zinc, homocysteine, and methyltetrahydrofolate."; RL J. Biol. Chem. 279:44235-44238(2004). CC -!- FUNCTION: Catalyzes the transfer of a methyl group from 5- CC methyltetrahydrofolate to homocysteine resulting in methionine CC formation. {ECO:0000269|PubMed:15024005}. CC -!- CATALYTIC ACTIVITY: CC Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = CC tetrahydropteroyltri-L-glutamate + L-methionine; CC Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, CC ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14; CC Evidence={ECO:0000269|PubMed:15024005}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:15326182}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:15326182}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=60 uM for 5-methyltetrahydrofolate {ECO:0000269|PubMed:15024005}; CC Vmax=26.5 nmol/min/mg enzyme toward 5-methyltetrahydrofolate CC {ECO:0000269|PubMed:15024005}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo CC pathway; L-methionine from L-homocysteine (MetE route): step 1/1. CC {ECO:0000269|PubMed:15024005}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15024005}. CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, flowers, siliques and CC seeds. {ECO:0000269|PubMed:15024005}. CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine synthase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U97200; AAC50037.1; -; mRNA. DR EMBL; AJ608673; CAE55863.1; -; mRNA. DR EMBL; AB011480; BAB11226.1; -; Genomic_DNA. DR EMBL; CP002688; AED92486.1; -; Genomic_DNA. DR EMBL; CP002688; AED92487.1; -; Genomic_DNA. DR EMBL; OZ408687; CAO7052657.1; -; Genomic_DNA. DR EMBL; AF370522; AAK43899.1; -; mRNA. DR EMBL; AY048201; AAK82464.1; -; mRNA. DR EMBL; AY056098; AAL06986.1; -; mRNA. DR EMBL; AY057478; AAL09712.1; -; mRNA. DR EMBL; AY057499; AAL09740.1; -; mRNA. DR EMBL; AY069876; AAL47432.1; -; mRNA. DR EMBL; AY070771; AAL50108.1; -; mRNA. DR EMBL; AY091692; AAM10291.1; -; mRNA. DR EMBL; BT000691; AAN31836.1; -; mRNA. DR PDB; 1U1H; X-ray; 2.55 A; A=1-765. DR PDB; 1U1J; X-ray; 2.40 A; A=1-765. DR PDB; 1U1U; X-ray; 2.95 A; A=1-765. DR PDB; 1U22; X-ray; 2.65 A; A=1-765. DR AlphaFoldDB; O50008; -. DR SMR; O50008; -. DR BioGRID; 16936; 14. DR FunCoup; O50008; 1676. DR IntAct; O50008; 2. DR MINT; O50008; -. DR STRING; 3702.O50008; -. DR iPTMnet; O50008; -. DR MetOSite; O50008; -. DR PaxDb; 3702-O50008; -. DR ProteomicsDB; 238988; -. DR KEGG; ath:AT5G17920; -. DR Araport; AT5G17920; -. DR TAIR; AT5G17920; ATMS1. DR eggNOG; KOG2263; Eukaryota. DR HOGENOM; CLU_013175_0_0_1; -. DR InParanoid; O50008; -. DR OMA; KVMKGML; -. DR PhylomeDB; O50008; -. DR BioCyc; ARA:AT5G17920-MONOMER; -. DR BRENDA; 2.1.1.14; 399. DR SABIO-RK; O50008; -. DR UniPathway; UPA00051; UER00082. DR CD-CODE; 4299E36E; Nucleolus. DR EvolutionaryTrace; O50008; -. DR PRO; PR:O50008; -. DR Proteomes; UP000006548; Chromosome 5. DR ExpressionAtlas; O50008; baseline and differential. DR GO; GO:0048046; C:apoplast; HDA:TAIR. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR. DR GO; GO:0005737; C:cytoplasm; ISM:TAIR. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:TAIR. DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0009506; C:plasmodesma; HDA:TAIR. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; HDA:TAIR. DR GO; GO:0008705; F:methionine synthase activity; IDA:TAIR. DR GO; GO:0003729; F:mRNA binding; IDA:TAIR. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IDA:UniProtKB. DR GO; GO:0006346; P:DNA methylation-dependent constitutive heterochromatin formation; IMP:TAIR. DR GO; GO:0071265; P:L-methionine biosynthetic process; IDA:TAIR. DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR. DR CDD; cd03311; CIMS_C_terminal_like; 1. DR CDD; cd03312; CIMS_N_terminal_like; 1. DR DisProt; DP03140; -. DR FunFam; 3.20.20.210:FF:000002; 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; 1. DR FunFam; 3.20.20.210:FF:000003; 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase; 1. DR Gene3D; 3.20.20.210; -; 2. DR HAMAP; MF_00172; Meth_synth; 1. DR InterPro; IPR013215; Cbl-indep_Met_Synth_N. DR InterPro; IPR006276; Cobalamin-indep_Met_synthase. DR InterPro; IPR002629; Met_Synth_C/arc. DR InterPro; IPR038071; UROD/MetE-like_sf. DR NCBIfam; TIGR01371; met_syn_B12ind; 1. DR NCBIfam; NF003556; PRK05222.1; 1. DR PANTHER; PTHR30519; 5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE; 1. DR Pfam; PF08267; Meth_synt_1; 1. DR Pfam; PF01717; Meth_synt_2; 1. DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1. DR SUPFAM; SSF51726; UROD/MetE-like; 2. DR PDBsum; 1U1H; -. DR PDBsum; 1U1J; -. DR PDBsum; 1U1U; -. DR PDBsum; 1U22; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW Transferase; Zinc. FT CHAIN 1..765 FT /note="5-methyltetrahydropteroyltriglutamate--homocysteine FT methyltransferase 1" FT /id="PRO_0000098696" FT ACT_SITE 701 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P82610" FT BINDING 18 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1J, ECO:0007744|PDB:1U22" FT BINDING 116 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1J" FT BINDING 437..439 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U22" FT BINDING 437..439 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J" FT BINDING 490 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J" FT BINDING 521..522 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1J, ECO:0007744|PDB:1U22" FT BINDING 567 FT /ligand="5-methyltetrahydropteroyltri-L-glutamate" FT /ligand_id="ChEBI:CHEBI:58207" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1J, ECO:0007744|PDB:1U22" FT BINDING 605 FT /ligand="L-homocysteine" FT /ligand_id="ChEBI:CHEBI:58199" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U22" FT BINDING 605 FT /ligand="L-methionine" FT /ligand_id="ChEBI:CHEBI:57844" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J" FT BINDING 647 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, FT ECO:0007744|PDB:1U1U, ECO:0007744|PDB:1U22" FT BINDING 649 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, FT ECO:0007744|PDB:1U22" FT BINDING 658 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, FT ECO:0007744|PDB:1U1U, ECO:0007744|PDB:1U22" FT BINDING 662 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, FT ECO:0007744|PDB:1U1U, ECO:0007744|PDB:1U22" FT BINDING 671 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P82610" FT BINDING 733 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000269|PubMed:15326182, FT ECO:0007744|PDB:1U1H, ECO:0007744|PDB:1U1J, FT ECO:0007744|PDB:1U22" FT CONFLICT 270 FT /note="R -> L (in Ref. 7; AAL09712)" FT /evidence="ECO:0000305" FT CONFLICT 282 FT /note="F -> S (in Ref. 3; CAE55863)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="G -> R (in Ref. 7; AAN31836)" FT /evidence="ECO:0000305" FT CONFLICT 351 FT /note="L -> M (in Ref. 3; CAE55863)" FT /evidence="ECO:0000305" FT CONFLICT 442 FT /note="Q -> R (in Ref. 7; AAN31836)" FT /evidence="ECO:0000305" FT HELIX 16..26 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 31..51 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 58..60 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 91..99 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:1U1H" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 136..146 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 152..156 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 158..163 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:1U1U" FT HELIX 177..180 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 181..197 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 202..206 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 216..228 FT /evidence="ECO:0007829|PDB:1U1J" FT TURN 230..233 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 249..255 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 263..270 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 274..280 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 303..316 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 322..328 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 337..339 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 345..348 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 354..369 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 374..389 FT /evidence="ECO:0007829|PDB:1U1J" FT TURN 391..393 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 397..400 FT /evidence="ECO:0007829|PDB:1U1J" FT TURN 401..405 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:1U1H" FT HELIX 416..418 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 420..426 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 463..479 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 484..486 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 498..501 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 504..508 FT /evidence="ECO:0007829|PDB:1U22" FT STRAND 515..518 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 541..546 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 554..559 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 561..566 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 568..570 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 572..574 FT /evidence="ECO:0007829|PDB:1U1H" FT HELIX 576..596 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 601..605 FT /evidence="ECO:0007829|PDB:1U1J" FT TURN 607..612 FT /evidence="ECO:0007829|PDB:1U1H" FT HELIX 617..619 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 620..635 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 640..647 FT /evidence="ECO:0007829|PDB:1U1J" FT TURN 654..656 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 657..661 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 666..669 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 672..675 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 679..683 FT /evidence="ECO:0007829|PDB:1U1J" FT TURN 684..687 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 691..693 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 696..698 FT /evidence="ECO:0007829|PDB:1U1J" FT STRAND 702..704 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 705..707 FT /evidence="ECO:0007829|PDB:1U1U" FT HELIX 708..720 FT /evidence="ECO:0007829|PDB:1U1J" FT TURN 724..726 FT /evidence="ECO:0007829|PDB:1U1H" FT STRAND 735..738 FT /evidence="ECO:0007829|PDB:1U1J" FT HELIX 740..759 FT /evidence="ECO:0007829|PDB:1U1J" SQ SEQUENCE 765 AA; 84357 MW; 2EA01908B5951154 CRC64; MASHIVGYPR MGPKRELKFA LESFWDGKST AEDLQKVSAD LRSSIWKQMS AAGTKFIPSN TFAHYDQVLD TTAMLGAVPP RYGYTGGEIG LDVYFSMARG NASVPAMEMT KWFDTNYHYI VPELGPEVNF SYASHKAVNE YKEAKALGVD TVPVLVGPVS YLLLSKAAKG VDKSFELLSL LPKILPIYKE VITELKAAGA TWIQLDEPVL VMDLEGQKLQ AFTGAYAELE STLSGLNVLV ETYFADIPAE AYKTLTSLKG VTAFGFDLVR GTKTLDLVKA GFPEGKYLFA GVVDGRNIWA NDFAASLSTL QALEGIVGKD KLVVSTSCSL LHTAVDLINE TKLDDEIKSW LAFAAQKVVE VNALAKALAG QKDEALFSAN AAALASRRSS PRVTNEGVQK AAAALKGSDH RRATNVSARL DAQQKKLNLP ILPTTTIGSF PQTVELRRVR REYKAKKVSE EDYVKAIKEE IKKVVDLQEE LDIDVLVHGE PERNDMVEYF GEQLSGFAFT ANGWVQSYGS RCVKPPVIYG DVSRPKAMTV FWSAMAQSMT SRPMKGMLTG PVTILNWSFV RNDQPRHETC YQIALAIKDE VEDLEKGGIG VIQIDEAALR EGLPLRKSEH AFYLDWAVHS FRITNCGVQD STQIHTHMCY SHFNDIIHSI IDMDADVITI ENSRSDEKLL SVFREGVKYG AGIGPGVYDI HSPRIPSSEE IADRVNKMLA VLEQNILWVN PDCGLKTRKY TEVKPALKNM VDAAKLIRSQ LASAK //