LDOX_ARATH
ID LDOX_ARATH Reviewed; 356 AA.
AC Q96323;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Leucoanthocyanidin dioxygenase;
DE Short=LDOX;
DE Short=Leucocyanidin oxygenase;
DE EC=1.14.20.4 {ECO:0000269|PubMed:16153644};
DE AltName: Full=Anthocyanidin synthase;
DE Short=ANS;
DE AltName: Full=Leucoanthocyanidin hydroxylase;
DE AltName: Full=Protein TANNIN DEFICIENT SEED 4;
DE Short=TDS4;
DE AltName: Full=Protein TRANSPARENT TESTA 11;
DE Short=TT11;
DE AltName: Full=Protein TRANSPARENT TESTA 17;
DE Short=TT17;
DE AltName: Full=Protein TRANSPARENT TESTA 18;
DE Short=TT18;
GN Name=LDOX; OrderedLocusNames=At4g22880; ORFNames=F7H19.60;
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 INDUCTION BY LIGHT.
RC STRAIN=cv. Columbia;
RX PubMed=9112784; DOI=10.1104/pp.113.4.1437;
RA Pelletier M.K., Murrell J.R., Shirley B.W.;
RT "Characterization of flavonol synthase and leucoanthocyanidin dioxygenase
RT genes in Arabidopsis. Further evidence for differential regulation of
RT 'early' and 'late' genes.";
RL Plant Physiol. 113:1437-1445(1997).
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].
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=10394944; DOI=10.1023/a:1026414301100;
RA Pelletier M.K., Burbulis I.E., Winkel-Shirley B.;
RT "Disruption of specific flavonoid genes enhances the accumulation of
RT flavonoid enzymes and end-products in Arabidopsis seedlings.";
RL Plant Mol. Biol. 40:45-54(1999).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-228.
RC STRAIN=cv. Wassilewskija-4;
RX PubMed=12940955; DOI=10.1046/j.1365-313x.2003.01834.x;
RA Abrahams S., Lee E., Walker A.R., Tanner G.J., Larkin P.J., Ashton A.R.;
RT "The Arabidopsis TDS4 gene encodes leucoanthocyanidin dioxygenase (LDOX)
RT and is essential for proanthocyanidin synthesis and vacuole development.";
RL Plant J. 35:624-636(2003).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16153644; DOI=10.1016/j.febslet.2005.08.033;
RA Welford R.W., Kirkpatrick J.M., McNeill L.A., Puri M., Oldham N.J.,
RA Schofield C.J.;
RT "Incorporation of oxygen into the succinate co-product of iron(II) and 2-
RT oxoglutarate dependent oxygenases from bacteria, plants and humans.";
RL FEBS Lett. 579:5170-5174(2005).
RN [8]
RP INDUCTION BY SUCROSE.
RX PubMed=16384906; DOI=10.1104/pp.105.072579;
RA Solfanelli C., Poggi A., Loreti E., Alpi A., Perata P.;
RT "Sucrose-specific induction of the anthocyanin biosynthetic pathway in
RT Arabidopsis.";
RL Plant Physiol. 140:637-646(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19433090; DOI=10.1016/j.febslet.2009.05.006;
RA Preuss A., Stracke R., Weisshaar B., Hillebrecht A., Matern U., Martens S.;
RT "Arabidopsis thaliana expresses a second functional flavonol synthase.";
RL FEBS Lett. 583:1981-1986(2009).
RN [10]
RP INDUCTION.
RX PubMed=19596700; DOI=10.1093/jxb/erp223;
RA Shan X., Zhang Y., Peng W., Wang Z., Xie D.;
RT "Molecular mechanism for jasmonate-induction of anthocyanin accumulation in
RT Arabidopsis.";
RL J. Exp. Bot. 60:3849-3860(2009).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-78; CYS-220 AND
RP GLY-228.
RC STRAIN=cv. Est-1, cv. Landsberg erecta, and cv. Wassilewskija-4;
RX PubMed=21683773; DOI=10.1016/j.gene.2011.05.031;
RA Appelhagen I., Jahns O., Bartelniewoehner L., Sagasser M., Weisshaar B.,
RA Stracke R.;
RT "Leucoanthocyanidin dioxygenase in Arabidopsis thaliana: characterization
RT of mutant alleles and regulation by MYB-BHLH-TTG1 transcription factor
RT complexes.";
RL Gene 484:61-68(2011).
RN [12]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE ANALOG
RP DIHYDROQUERCETIN; 2-OXOGLUTARATE AND IRON ION, AND COFACTOR.
RX PubMed=11796114; DOI=10.1016/s0969-2126(01)00695-5;
RA Wilmouth R.C., Turnbull J.J., Welford R.W., Clifton I.J., Prescott A.G.,
RA Schofield C.J.;
RT "Structure and mechanism of anthocyanidin synthase from Arabidopsis
RT thaliana.";
RL Structure 10:93-103(2002).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-356 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG NARINGENIN; 2-OXOGLUTARATE AND IRON ION, FUNCTION,
RP COFACTOR, AND MUTAGENESIS OF LYS-128; ASN-131; TYR-142; GLU-230 AND
RP LYS-341.
RX PubMed=16106293; DOI=10.1039/b507153d;
RA Welford R.W., Clifton I.J., Turnbull J.J., Wilson S.C., Schofield C.J.;
RT "Structural and mechanistic studies on anthocyanidin synthase catalysed
RT oxidation of flavanone substrates: the effect of C-2 stereochemistry on
RT product selectivity and mechanism.";
RL Org. Biomol. Chem. 3:3117-3126(2005).
CC -!- FUNCTION: Involved in anthocyanin and protoanthocyanidin biosynthesis
CC by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins.
CC Possesses low flavonol synthase activity in vitro towards
CC dihydrokaempferol and dihydroquercetin producing kaempferol and
CC quercitin, respectively. {ECO:0000269|PubMed:12940955,
CC ECO:0000269|PubMed:16106293, ECO:0000269|PubMed:16153644,
CC ECO:0000269|PubMed:19433090, ECO:0000269|PubMed:21683773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a (2R,3S,4S)-leucoanthocyanidin + O2 = a 4-H-
CC anthocyanidin with a 3-hydroxy group + CO2 + 2 H2O + succinate;
CC Xref=Rhea:RHEA:54432, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:138176, ChEBI:CHEBI:138177; EC=1.14.20.4;
CC Evidence={ECO:0000269|PubMed:16153644};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S,4S)-3,4-leucopelargonidin + 2-oxoglutarate + O2 = (4S)-
CC 2,3-dehydroleucopelargonidin + CO2 + H(+) + H2O + succinate;
CC Xref=Rhea:RHEA:10768, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17343, ChEBI:CHEBI:30031, ChEBI:CHEBI:138950;
CC EC=1.14.20.4; Evidence={ECO:0000269|PubMed:16153644};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S,4S)-leucocyanidin + 2-oxoglutarate + O2 = (4S)-2,3-
CC dehydroleucocyanidin + CO2 + H(+) + H2O + succinate;
CC Xref=Rhea:RHEA:10764, ChEBI:CHEBI:11412, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138948;
CC EC=1.14.20.4; Evidence={ECO:0000269|PubMed:16153644};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000269|PubMed:11796114, ECO:0000269|PubMed:16106293};
CC Note=Binds 1 ascorbate molecule per subunit.
CC {ECO:0000269|PubMed:11796114, ECO:0000269|PubMed:16106293};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:11796114, ECO:0000269|PubMed:16106293};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:11796114,
CC ECO:0000269|PubMed:16106293};
CC -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings (at protein level).
CC {ECO:0000269|PubMed:10394944}.
CC -!- INDUCTION: By methyl jasmonate, 6-benzylaminopurine, light and sucrose.
CC {ECO:0000269|PubMed:16384906, ECO:0000269|PubMed:19596700,
CC ECO:0000269|PubMed:9112784}.
CC -!- DISRUPTION PHENOTYPE: No accumulation of anthocyanins, accumulation of
CC protoanthocyanidin intermediates and presence of numerous small
CC vacuoles in leaf epidermal cells. {ECO:0000269|PubMed:12940955,
CC ECO:0000269|PubMed:19433090, ECO:0000269|PubMed:21683773}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; U70478; AAB09572.1; -; mRNA.
DR EMBL; AL031018; CAA19803.1; -; Genomic_DNA.
DR EMBL; AL161558; CAB79243.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84672.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84673.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67022.1; -; Genomic_DNA.
DR EMBL; AY088203; AAM65745.1; -; mRNA.
DR PIR; T05119; T05119.
DR RefSeq; NP_001031700.1; NM_001036623.1.
DR RefSeq; NP_001320035.1; NM_001341563.1.
DR RefSeq; NP_194019.1; NM_118417.2.
DR PDB; 1GP4; X-ray; 2.10 A; A=1-356.
DR PDB; 1GP5; X-ray; 2.20 A; A=1-356.
DR PDB; 1GP6; X-ray; 1.75 A; A=1-356.
DR PDB; 2BRT; X-ray; 2.20 A; A=2-356.
DR PDBsum; 1GP4; -.
DR PDBsum; 1GP5; -.
DR PDBsum; 1GP6; -.
DR PDBsum; 2BRT; -.
DR AlphaFoldDB; Q96323; -.
DR SMR; Q96323; -.
DR BioGRID; 13676; 1.
DR STRING; 3702.AT4G22880.1; -.
DR iPTMnet; Q96323; -.
DR PaxDb; Q96323; -.
DR PRIDE; Q96323; -.
DR ProteomicsDB; 237135; -.
DR EnsemblPlants; AT4G22880.1; AT4G22880.1; AT4G22880.
DR EnsemblPlants; AT4G22880.2; AT4G22880.2; AT4G22880.
DR EnsemblPlants; AT4G22880.3; AT4G22880.3; AT4G22880.
DR GeneID; 828387; -.
DR Gramene; AT4G22880.1; AT4G22880.1; AT4G22880.
DR Gramene; AT4G22880.2; AT4G22880.2; AT4G22880.
DR Gramene; AT4G22880.3; AT4G22880.3; AT4G22880.
DR KEGG; ath:AT4G22880; -.
DR Araport; AT4G22880; -.
DR TAIR; locus:2127218; AT4G22880.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_2_1; -.
DR InParanoid; Q96323; -.
DR OMA; REDRISM; -.
DR OrthoDB; 830141at2759; -.
DR PhylomeDB; Q96323; -.
DR BioCyc; ARA:AT4G22880-MON; -.
DR BioCyc; MetaCyc:AT4G22880-MON; -.
DR BRENDA; 1.14.20.4; 399.
DR UniPathway; UPA00009; -.
DR EvolutionaryTrace; Q96323; -.
DR PRO; PR:Q96323; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q96323; baseline and differential.
DR Genevisible; Q96323; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0050589; F:leucocyanidin oxygenase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; TAS:TAIR.
DR GO; GO:0010023; P:proanthocyanidin biosynthetic process; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0007033; P:vacuole organization; IMP:TAIR.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Vitamin C.
FT CHAIN 1..356
FT /note="Leucoanthocyanidin dioxygenase"
FT /id="PRO_0000067299"
FT DOMAIN 208..307
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 215..217
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 288
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 298..300
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 306
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11796114,
FT ECO:0000269|PubMed:16106293"
FT MUTAGEN 78
FT /note="G->E: In tt11-2; no accumulation of anthocyanin."
FT /evidence="ECO:0000269|PubMed:21683773"
FT MUTAGEN 128
FT /note="K->A: Retains two-third of the original activity."
FT /evidence="ECO:0000269|PubMed:16106293"
FT MUTAGEN 131
FT /note="N->A,D: Retains two-third of the original activity."
FT /evidence="ECO:0000269|PubMed:16106293"
FT MUTAGEN 142
FT /note="Y->H: Retains two-third of the original activity."
FT /evidence="ECO:0000269|PubMed:16106293"
FT MUTAGEN 220
FT /note="C->Y: In tt17; no accumulation of anthocyanin."
FT /evidence="ECO:0000269|PubMed:21683773"
FT MUTAGEN 228
FT /note="G->D: In tds4-1; no accumulation of anthocyanin."
FT /evidence="ECO:0000269|PubMed:12940955,
FT ECO:0000269|PubMed:21683773"
FT MUTAGEN 230
FT /note="E->Q: Retains one half of the original activity."
FT /evidence="ECO:0000269|PubMed:16106293"
FT MUTAGEN 341
FT /note="K->N: Retains two-third of the original activity."
FT /evidence="ECO:0000269|PubMed:16106293"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1GP6"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 89..103
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:2BRT"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 165..190
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:1GP6"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1GP6"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:1GP6"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1GP6"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:1GP6"
FT HELIX 334..349
FT /evidence="ECO:0007829|PDB:1GP6"
SQ SEQUENCE 356 AA; 40396 MW; 1B74AE3A54056201 CRC64;
MVAVERVESL AKSGIISIPK EYIRPKEELE SINDVFLEEK KEDGPQVPTI DLKNIESDDE
KIRENCIEEL KKASLDWGVM HLINHGIPAD LMERVKKAGE EFFSLSVEEK EKYANDQATG
KIQGYGSKLA NNASGQLEWE DYFFHLAYPE EKRDLSIWPK TPSDYIEATS EYAKCLRLLA
TKVFKALSVG LGLEPDRLEK EVGGLEELLL QMKINYYPKC PQPELALGVE AHTDVSALTF
ILHNMVPGLQ LFYEGKWVTA KCVPDSIVMH IGDTLEILSN GKYKSILHRG LVNKEKVRIS
WAVFCEPPKD KIVLKPLPEM VSVESPAKFP PRTFAQHIEH KLFGKEQEEL VSEKND
