METE1_ARATH
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 03-AUG-2022, entry version 170.
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 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 [7] {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 = L-
CC methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199,
CC 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}.
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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; 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 RefSeq; NP_001078599.1; NM_001085130.2.
DR RefSeq; NP_197294.1; NM_121798.4.
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 PDBsum; 1U1H; -.
DR PDBsum; 1U1J; -.
DR PDBsum; 1U1U; -.
DR PDBsum; 1U22; -.
DR AlphaFoldDB; O50008; -.
DR SMR; O50008; -.
DR BioGRID; 16936; 14.
DR IntAct; O50008; 2.
DR MINT; O50008; -.
DR STRING; 3702.AT5G17920.1; -.
DR iPTMnet; O50008; -.
DR MetOSite; O50008; -.
DR SWISS-2DPAGE; O50008; -.
DR PaxDb; O50008; -.
DR PRIDE; O50008; -.
DR ProteomicsDB; 238988; -.
DR EnsemblPlants; AT5G17920.1; AT5G17920.1; AT5G17920.
DR EnsemblPlants; AT5G17920.2; AT5G17920.2; AT5G17920.
DR GeneID; 831660; -.
DR Gramene; AT5G17920.1; AT5G17920.1; AT5G17920.
DR Gramene; AT5G17920.2; AT5G17920.2; AT5G17920.
DR KEGG; ath:AT5G17920; -.
DR Araport; AT5G17920; -.
DR TAIR; locus:2170318; AT5G17920.
DR eggNOG; KOG2263; Eukaryota.
DR HOGENOM; CLU_013175_0_0_1; -.
DR InParanoid; O50008; -.
DR OMA; KVMKGML; -.
DR OrthoDB; 237390at2759; -.
DR PhylomeDB; O50008; -.
DR BioCyc; ARA:AT5G17920-MON; -.
DR BRENDA; 2.1.1.14; 399.
DR SABIO-RK; O50008; -.
DR UniPathway; UPA00051; UER00082.
DR EvolutionaryTrace; O50008; -.
DR PRO; PR:O50008; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O50008; baseline and differential.
DR Genevisible; O50008; AT.
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: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 heterochromatin assembly; IMP:TAIR.
DR GO; GO:0009086; P:methionine biosynthetic process; IDA:TAIR.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IEP:TAIR.
DR CDD; cd03311; CIMS_C_terminal_like; 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 Pfam; PF08267; Meth_synt_1; 1.
DR Pfam; PF01717; Meth_synt_2; 1.
DR PIRSF; PIRSF000382; MeTrfase_B12_ind; 1.
DR SUPFAM; SSF51726; SSF51726; 2.
DR TIGRFAMs; TIGR01371; met_syn_B12ind; 1.
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. 6; 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. 6; 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. 6; 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 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 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..368
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 708..720
FT /evidence="ECO:0007829|PDB:1U1J"
FT STRAND 724..727
FT /evidence="ECO:0007829|PDB:1U22"
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
