PAT_ARATH
ID PAT_ARATH Reviewed; 475 AA.
AC Q9SIE1; E9L7A7; Q3E6N9; Q8LFX1; Q8VZI1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase;
DE Short=AtAAT;
DE Short=AtPPA-AT;
DE EC=2.6.1.1;
DE EC=2.6.1.78;
DE EC=2.6.1.79;
DE AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 17;
DE Flags: Precursor;
GN Name=PAT; Synonyms=AAT, MEE17; OrderedLocusNames=At2g22250;
GN ORFNames=T26C19.9;
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 BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21102469; DOI=10.1038/nchembio.485;
RA Maeda H., Yoo H., Dudareva N.;
RT "Prephenate aminotransferase directs plant phenylalanine biosynthesis via
RT arogenate.";
RL Nat. Chem. Biol. 7:19-21(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [7]
RP FUNCTION.
RX PubMed=15634699; DOI=10.1242/dev.01595;
RA Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S., Johnson C.S.,
RA Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT "Genetic and molecular identification of genes required for female
RT gametophyte development and function in Arabidopsis.";
RL Development 132:603-614(2005).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16623902; DOI=10.1111/j.1365-313x.2006.02713.x;
RA de la Torre F., De Santis L., Suarez M.F., Crespillo R., Canovas F.M.;
RT "Identification and functional analysis of a prokaryotic-type aspartate
RT aminotransferase: implications for plant amino acid metabolism.";
RL Plant J. 46:414-425(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20883697; DOI=10.1016/j.febslet.2010.09.037;
RA Graindorge M., Giustini C., Jacomin A.C., Kraut A., Curien G., Matringe M.;
RT "Identification of a plant gene encoding glutamate/aspartate-prephenate
RT aminotransferase: The last homeless enzyme of aromatic amino acids
RT biosynthesis.";
RL FEBS Lett. 584:4357-4360(2010).
CC -!- FUNCTION: Prokaryotic-type aspartate aminotransferase. Has also a
CC prenate transaminase activity. Involved in the aromatic amino acids
CC biosynthesis pathway via the arogenate route. Required for the
CC transamination of prephenate into arogenate. Required for early
CC development of the embryo. {ECO:0000269|PubMed:15634699,
CC ECO:0000269|PubMed:16623902, ECO:0000269|PubMed:20883697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC Evidence={ECO:0000269|PubMed:20883697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arogenate + oxaloacetate = L-aspartate + prephenate;
CC Xref=Rhea:RHEA:20445, ChEBI:CHEBI:16452, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58180; EC=2.6.1.78;
CC Evidence={ECO:0000269|PubMed:20883697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-arogenate = L-glutamate + prephenate;
CC Xref=Rhea:RHEA:22880, ChEBI:CHEBI:16810, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58180; EC=2.6.1.79;
CC Evidence={ECO:0000269|PubMed:20883697};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12 mM for aspartate for the asparte aminotransferase activity
CC {ECO:0000269|PubMed:20883697, ECO:0000269|PubMed:21102469};
CC KM=5.6 mM for glutamate for the asparte aminotransferase activity
CC {ECO:0000269|PubMed:20883697, ECO:0000269|PubMed:21102469};
CC KM=25 uM for oxaloacetate for the asparte aminotransferase activity
CC {ECO:0000269|PubMed:20883697, ECO:0000269|PubMed:21102469};
CC KM=200 uM for 2-oxoglutarate for the asparte aminotransferase
CC activity {ECO:0000269|PubMed:20883697, ECO:0000269|PubMed:21102469};
CC KM=14 uM for prephenate for the prephenate aminotransferase activity
CC {ECO:0000269|PubMed:20883697, ECO:0000269|PubMed:21102469};
CC KM=1.5 mM for glutamate for the prephenate aminotransferase activity
CC {ECO:0000269|PubMed:20883697, ECO:0000269|PubMed:21102469};
CC KM=2.2 mM for aspartate for the prephenate aminotransferase activity
CC {ECO:0000269|PubMed:20883697, ECO:0000269|PubMed:21102469};
CC KM=355 uM for prephenate (for the recombinant enzyme with 20 mM
CC aspartate as cosubstrate) {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC KM=684 uM for prephenate (for the recombinant enzyme with 20 mM
CC glutamate as cosubstrate) {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC KM=691 uM for 2-oxoglutarate (for the recombinant enzyme with 20 mM
CC aspartate as cosubstrate) {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC KM=2.69 mM for glutamate (for the recombinant enzyme with 3 mM
CC prephenate as cosubstrate) {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC KM=2.84 mM for aspartate (for the recombinant enzyme with 3 mM
CC prephenate as cosubstrate) {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC KM=8.22 mM for oxaloacetate (for the recombinant enzyme with 20 mM
CC glutamate as cosubstrate) {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC Vmax=88 nmol/sec/mg enzyme toward prephenate with 20 mM aspartate as
CC cosubstrate {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC Vmax=173 nmol/sec/mg enzyme toward prephenate with 20 mM glutamate as
CC cosubstrate {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC Vmax=325 nmol/sec/mg enzyme toward 2-oxoglutarate with 20 mM
CC aspartate as cosubstrate {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC Vmax=90 nmol/sec/mg enzyme toward glutamate with 3 mM prephenate as
CC cosubstrate {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC Vmax=70 nmol/sec/mg enzyme toward aspartate with 3 mM prephenate as
CC cosubstrate {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC Vmax=3.29 umol/sec/mg enzyme toward oxaloacetate with 20 mM glutamate
CC as cosubstrate {ECO:0000269|PubMed:20883697,
CC ECO:0000269|PubMed:21102469};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC arogenate from prephenate (L-Asp route): step 1/1.
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-
CC arogenate from prephenate (L-Glu route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16623902}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIE1-2; Sequence=VSP_040191;
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; HM638413; ADM67558.1; -; mRNA.
DR EMBL; AC007168; AAD23617.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07283.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07284.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07285.1; -; Genomic_DNA.
DR EMBL; AY064152; AAL36058.1; -; mRNA.
DR EMBL; AY124811; AAM70520.1; -; mRNA.
DR EMBL; AY084599; AAM61164.1; -; mRNA.
DR EMBL; BX820081; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; E84610; E84610.
DR RefSeq; NP_001031394.1; NM_001036317.1. [Q9SIE1-1]
DR RefSeq; NP_565529.1; NM_127791.3. [Q9SIE1-1]
DR RefSeq; NP_850022.1; NM_179691.4. [Q9SIE1-2]
DR PDB; 5WMH; X-ray; 3.00 A; A/B/C/D/E/F=1-475.
DR PDB; 5WMI; X-ray; 2.00 A; A=1-475.
DR PDB; 5WMK; X-ray; 1.40 A; A=1-475.
DR PDB; 5WML; X-ray; 2.10 A; A/B=1-475.
DR PDB; 6F5V; X-ray; 1.70 A; A/B/C/D=1-475.
DR PDBsum; 5WMH; -.
DR PDBsum; 5WMI; -.
DR PDBsum; 5WMK; -.
DR PDBsum; 5WML; -.
DR PDBsum; 6F5V; -.
DR AlphaFoldDB; Q9SIE1; -.
DR SMR; Q9SIE1; -.
DR BioGRID; 2111; 2.
DR STRING; 3702.AT2G22250.2; -.
DR PaxDb; Q9SIE1; -.
DR PRIDE; Q9SIE1; -.
DR ProteomicsDB; 248639; -. [Q9SIE1-1]
DR EnsemblPlants; AT2G22250.1; AT2G22250.1; AT2G22250. [Q9SIE1-2]
DR EnsemblPlants; AT2G22250.2; AT2G22250.2; AT2G22250. [Q9SIE1-1]
DR EnsemblPlants; AT2G22250.3; AT2G22250.3; AT2G22250. [Q9SIE1-1]
DR GeneID; 816758; -.
DR Gramene; AT2G22250.1; AT2G22250.1; AT2G22250. [Q9SIE1-2]
DR Gramene; AT2G22250.2; AT2G22250.2; AT2G22250. [Q9SIE1-1]
DR Gramene; AT2G22250.3; AT2G22250.3; AT2G22250. [Q9SIE1-1]
DR KEGG; ath:AT2G22250; -.
DR Araport; AT2G22250; -.
DR TAIR; locus:2060435; AT2G22250.
DR eggNOG; KOG0257; Eukaryota.
DR InParanoid; Q9SIE1; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q9SIE1; -.
DR BioCyc; ARA:AT2G22250-MON; -.
DR BRENDA; 2.6.1.1; 399.
DR BRENDA; 2.6.1.78; 399.
DR BRENDA; 2.6.1.79; 399.
DR SABIO-RK; Q9SIE1; -.
DR UniPathway; UPA00121; UER00342.
DR UniPathway; UPA00121; UER00343.
DR PRO; PR:Q9SIE1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIE1; baseline and differential.
DR Genevisible; Q9SIE1; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0033853; F:aspartate-prephenate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0033854; F:glutamate-prephenate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009095; P:aromatic amino acid family biosynthetic process, prephenate pathway; IDA:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Amino-acid biosynthesis;
KW Aminotransferase; Chloroplast; Plastid; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..55
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 56..475
FT /note="Bifunctional aspartate aminotransferase and
FT glutamate/aspartate-prephenate aminotransferase"
FT /id="PRO_0000401475"
FT BINDING 107
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 306
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040191"
FT CONFLICT 80
FT /note="K -> R (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="I -> M (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="T -> S (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> P (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="S -> L (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="L -> S (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="F -> L (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="F -> L (in Ref. 6; BX820081)"
FT /evidence="ECO:0000305"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 115..126
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 222..228
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 233..241
FT /evidence="ECO:0007829|PDB:5WMK"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:5WMK"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:5WMK"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:5WMK"
FT TURN 305..309
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 358..380
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 391..399
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:5WMK"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 417..428
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:5WMK"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 452..466
FT /evidence="ECO:0007829|PDB:5WMK"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:6F5V"
SQ SEQUENCE 475 AA; 51000 MW; 5F17130EE2533B38 CRC64;
MASQSSVAVI SSAAARGESF PDSKKPIGSV RFQQPLRLSF SYCKSGNMSS RICAMAKPND
AETLSSSVDM SLSPRVQSLK PSKTMVITDL AATLVQSGVP VIRLAAGEPD FDTPKVVAEA
GINAIREGFT RYTLNAGITE LREAICRKLK EENGLSYAPD QILVSNGAKQ SLLQAVLAVC
SPGDEVIIPA PYWVSYTEQA RLADATPVVI PTKISNNFLL DPKDLESKLT EKSRLLILCS
PSNPTGSVYP KSLLEEIARI IAKHPRLLVL SDEIYEHIIY APATHTSFAS LPDMYERTLT
VNGFSKAFAM TGWRLGYLAG PKHIVAACSK LQGQVSSGAS SIAQKAGVAA LGLGKAGGET
VAEMVKAYRE RRDFLVKSLG DIKGVKISEP QGAFYLFIDF SAYYGSEAEG FGLINDSSSL
ALYFLDKFQV AMVPGDAFGD DSCIRISYAT SLDVLQAAVE KIRKALEPLR ATVSV
