4CLLA_ARATH
ID 4CLLA_ARATH Reviewed; 514 AA.
AC Q9SMT7; Q8L9Z5;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Oxalate--CoA ligase {ECO:0000305};
DE EC=6.2.1.8 {ECO:0000269|PubMed:22447686};
DE AltName: Full=4-coumarate--CoA ligase isoform 8;
DE Short=At4CL8;
DE AltName: Full=4-coumarate--CoA ligase-like 10;
DE AltName: Full=Acyl-activating enzyme 3 {ECO:0000303|PubMed:22447686};
DE AltName: Full=Adenosine monophosphate binding protein 3 {ECO:0000303|PubMed:12177484};
DE Short=AtMPBP3 {ECO:0000303|PubMed:12177484};
DE AltName: Full=Oxalyl-CoA synthetase;
GN Name=AAE3 {ECO:0000303|PubMed:22447686};
GN Synonyms=4CLL10, AMPBP3 {ECO:0000303|PubMed:12177484};
GN OrderedLocusNames=At3g48990 {ECO:0000312|Araport:AT3G48990};
GN ORFNames=T2J13.170 {ECO:0000312|EMBL:CAB62011.1};
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 [MRNA].
RX PubMed=12177484; DOI=10.1104/pp.003269;
RA Shockey J.M., Fulda M.S., Browse J.A.;
RT "Arabidopsis contains nine long-chain acyl-coenzyme A synthetase genes that
RT participate in fatty acid and glycerolipid metabolism.";
RL Plant Physiol. 129:1710-1722(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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.
RX PubMed=12819348; DOI=10.1073/pnas.1430550100;
RA Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D.,
RA Kombrink E., Stuible H.-P.;
RT "The substrate specificity-determining amino acid code of 4-coumarate:CoA
RT ligase.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003).
RN [7]
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND INDUCTION BY PATHOGEN.
RC STRAIN=cv. Columbia;
RX PubMed=22447686; DOI=10.1105/tpc.112.096032;
RA Foster J., Kim H.U., Nakata P.A., Browse J.;
RT "A previously unknown oxalyl-CoA synthetase is important for oxalate
RT catabolism in Arabidopsis.";
RL Plant Cell 24:1217-1229(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH ATP AND OXALIC ACID,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-214; SER-289;
RP HIS-319; ARG-409 AND LYS-500.
RX PubMed=27326693; DOI=10.1016/j.molp.2016.06.002;
RA Fan M., Xiao Y., Li M., Chang W.;
RT "Crystal structures of Arabidopsis thaliana oxalyl-CoA synthetase essential
RT for oxalate degradation.";
RL Mol. Plant 9:1349-1352(2016).
CC -!- FUNCTION: Oxalyl-CoA synthetase acting exclusively against oxalate. No
CC activity with malonate, succinate, malate, acetate, formate, lactate,
CC glycolate, glyoxylate or glutarate. Required for oxalate degradation,
CC normal seed development and defense against oxalate-producing fungal
CC pathogens. {ECO:0000269|PubMed:22447686}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + oxalate = AMP + diphosphate + oxalyl-CoA;
CC Xref=Rhea:RHEA:18293, ChEBI:CHEBI:30616, ChEBI:CHEBI:30623,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57388,
CC ChEBI:CHEBI:456215; EC=6.2.1.8;
CC Evidence={ECO:0000269|PubMed:22447686};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=42 uM for oxalate {ECO:0000269|PubMed:27326693};
CC KM=149 uM for oxalate {ECO:0000269|PubMed:22447686};
CC Vmax=13.8 umol/min/mg enzyme {ECO:0000269|PubMed:27326693};
CC Vmax=11.4 umol/min/mg enzyme {ECO:0000269|PubMed:22447686};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:22447686};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22447686}.
CC -!- INDUCTION: Up-regulated upon infection with oxalate-producing fungal
CC pathogens. {ECO:0000269|PubMed:22447686}.
CC -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are involved in
CC the substrate recognition, and are sufficient to confer the substrate
CC specificity. {ECO:0000250|UniProtKB:Q42524}.
CC -!- DISRUPTION PHENOTYPE: Decreased and delayed seed germination, but no
CC other growth and development phenotypes. Increased sensitivity to
CC oxalate-producing fungal pathogens. {ECO:0000269|PubMed:22447686}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF503762; AAM28620.1; -; mRNA.
DR EMBL; AL132967; CAB62011.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78480.1; -; Genomic_DNA.
DR EMBL; AY050824; AAK92759.1; -; mRNA.
DR EMBL; AY062759; AAL32837.1; -; mRNA.
DR EMBL; AY117254; AAM51329.1; -; mRNA.
DR EMBL; BT003376; AAO30039.1; -; mRNA.
DR EMBL; AY088127; AAM65672.1; -; mRNA.
DR PIR; T46131; T46131.
DR RefSeq; NP_190468.1; NM_114758.5.
DR PDB; 5IE0; X-ray; 2.00 A; A/B=1-514.
DR PDB; 5IE2; X-ray; 1.85 A; A/B=1-514.
DR PDB; 5IE3; X-ray; 1.90 A; A/B=1-514.
DR PDBsum; 5IE0; -.
DR PDBsum; 5IE2; -.
DR PDBsum; 5IE3; -.
DR AlphaFoldDB; Q9SMT7; -.
DR SMR; Q9SMT7; -.
DR BioGRID; 9378; 5.
DR IntAct; Q9SMT7; 1.
DR STRING; 3702.AT3G48990.1; -.
DR iPTMnet; Q9SMT7; -.
DR PaxDb; Q9SMT7; -.
DR PRIDE; Q9SMT7; -.
DR ProteomicsDB; 244508; -.
DR EnsemblPlants; AT3G48990.1; AT3G48990.1; AT3G48990.
DR GeneID; 824060; -.
DR Gramene; AT3G48990.1; AT3G48990.1; AT3G48990.
DR KEGG; ath:AT3G48990; -.
DR Araport; AT3G48990; -.
DR TAIR; locus:2101368; AT3G48990.
DR eggNOG; KOG1176; Eukaryota.
DR HOGENOM; CLU_000022_59_0_1; -.
DR InParanoid; Q9SMT7; -.
DR OMA; PNIRFIR; -.
DR OrthoDB; 330201at2759; -.
DR PhylomeDB; Q9SMT7; -.
DR BioCyc; ARA:AT3G48990-MON; -.
DR BioCyc; MetaCyc:AT3G48990-MON; -.
DR BRENDA; 6.2.1.8; 399.
DR PRO; PR:Q9SMT7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SMT7; baseline and differential.
DR Genevisible; Q9SMT7; 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:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0050203; F:oxalate-CoA ligase activity; IDA:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0033611; P:oxalate catabolic process; IDA:TAIR.
DR GO; GO:0010030; P:positive regulation of seed germination; IMP:TAIR.
DR GO; GO:0010214; P:seed coat development; IMP:TAIR.
DR CDD; cd05926; FACL_fum10p_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR045310; Pcs60-like.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Plant defense; Reference proteome.
FT CHAIN 1..514
FT /note="Oxalate--CoA ligase"
FT /id="PRO_0000415617"
FT REGION 241..310
FT /note="SBD1"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT REGION 311..374
FT /note="SBD2"
FT /evidence="ECO:0000250|UniProtKB:Q42524"
FT BINDING 170..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2"
FT BINDING 289..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3"
FT BINDING 289
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE3"
FT BINDING 310..311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3"
FT BINDING 314
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE3"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3"
FT BINDING 319
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE3"
FT BINDING 394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3"
FT BINDING 409
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2"
FT BINDING 500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE2, ECO:0007744|PDB:5IE3"
FT BINDING 500
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:27326693,
FT ECO:0007744|PDB:5IE3"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 214
FT /note="H->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:27326693"
FT MUTAGEN 289
FT /note="S->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:27326693"
FT MUTAGEN 319
FT /note="H->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:27326693"
FT MUTAGEN 409
FT /note="R->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:27326693"
FT MUTAGEN 500
FT /note="K->A: Abolished activity."
FT /evidence="ECO:0000269|PubMed:27326693"
FT CONFLICT 137
FT /note="G -> V (in Ref. 5; AAM65672)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="V -> F (in Ref. 5; AAM65672)"
FT /evidence="ECO:0000305"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:5IE2"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 33..50
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 67..78
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 115..123
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5IE2"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 184..198
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:5IE2"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:5IE2"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 378..384
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 389..398
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 423..430
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 436..446
FT /evidence="ECO:0007829|PDB:5IE2"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 450..459
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 467..477
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:5IE2"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5IE2"
FT HELIX 503..510
FT /evidence="ECO:0007829|PDB:5IE2"
SQ SEQUENCE 514 AA; 55544 MW; DAF41A51D8934371 CRC64;
MDSDTLSGLL ENVAKKFPDR RALSVSGKFN LTHARLHDLI ERAASRLVSD AGIKPGDVVA
LTFPNTVEFV IMFLAVIRAR ATAAPLNAAY TAEEFEFYLS DSDSKLLLTS KEGNAPAQEA
ASKLKISHVT ATLLDAGSDL VLSVADSDSV VDSATELVNH PDDGALFLHT SGTTSRPKGV
PLTQLNLASS VKNIKAVYKL TESDSTVIVL PLFHVHGLLA GLLSSLGAGA AVTLPAAGRF
SATTFWPDMK KYNATWYTAV PTIHQIILDR HASHPETEYP KLRFIRSCSA SLAPVILSRL
EEAFGAPVLE AYAMTEATHL MSSNPLPEEG PHKPGSVGKP VGQEMAILNE KGEIQEPNNK
GEVCIRGPNV TKGYKNNPEA NKAGFEFGWF HTGDIGYFDT DGYLHLVGRI KELINRGGEK
ISPIEVDAVL LTHPDVSQGV AFGVPDEKYG EEINCAVIPR EGTTVTEEDI KAFCKKNLAA
FKVPKRVFIT DNLPKTASGK IQRRIVAQHF LEKP
