LOX1_SOYBN
ID LOX1_SOYBN Reviewed; 839 AA.
AC P08170;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Seed linoleate 13S-lipoxygenase-1;
DE EC=1.13.11.12 {ECO:0000269|PubMed:16157595, ECO:0000269|PubMed:2492826};
DE AltName: Full=Lipoxygenase-1;
DE Short=L-1;
GN Name=LOX1.1; Synonyms=LOX1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3112136; DOI=10.1016/s0021-9258(18)61079-8;
RA Shibata D., Steczko J., Dixon J.E., Hermodson M., Yazdanparast R.,
RA Axelrod B.;
RT "Primary structure of soybean lipoxygenase-1.";
RL J. Biol. Chem. 262:10080-10085(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Bonminori; TISSUE=Cotyledon;
RA Fukazawa C., Masayoshi M., Chikafusa F.;
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 426-752.
RX AGRICOLA=IND87003970; DOI=10.1007/BF00020127;
RA Start W.G., Ma Y., Polacco J.C., Hildebrand D.F., Freyer G.A.,
RA Altschuler M.;
RT "Two soybean seed lipoxygenase nulls accumulate reduced levels of
RT lipoxygenase transcripts.";
RL Plant Mol. Biol. 7:11-23(1986).
RN [4]
RP SEQUENCE REVISION TO 479-482, AND MUTAGENESIS OF SOME HISTIDINE RESIDUES.
RX PubMed=1567851; DOI=10.1021/bi00131a022;
RA Steczko J., Donoho G.P., Clemens J.C., Dixon J.E., Axelrod B.;
RT "Conserved histidine residues in soybean lipoxygenase: functional
RT consequences of their replacement.";
RL Biochemistry 31:4053-4057(1992).
RN [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SPECIFICITY.
RX PubMed=2492826; DOI=10.1016/0005-2760(89)90111-2;
RA Gardner H.W.;
RT "Soybean lipoxygenase-1 enzymically forms both (9S)- and (13S)-
RT hydroperoxides from linoleic acid by a pH-dependent mechanism.";
RL Biochim. Biophys. Acta 1001:274-281(1989).
RN [6]
RP MUTAGENESIS OF SOME HISTIDINE RESIDUES.
RX PubMed=1497657; DOI=10.1016/0006-291x(92)90801-q;
RA Steczko J., Axelrod B.;
RT "Identification of the iron-binding histidine residues in soybean
RT lipoxygenase L-1.";
RL Biochem. Biophys. Res. Commun. 186:686-689(1992).
RN [7]
RP COFACTOR.
RX PubMed=8518276; DOI=10.1021/bi00076a003;
RA Minor W., Steczko J., Bolin J.T., Otwinowski Z., Axelrod B.;
RT "Crystallographic determination of the active site iron and its ligands in
RT soybean lipoxygenase L-1.";
RL Biochemistry 32:6320-6323(1993).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ALA-542, ENZYME KINETICS,
RP REACTION MECHANISM, AND EPR SPECTROSCOPY.
RX PubMed=16157595; DOI=10.1074/jbc.m504870200;
RA Coffa G., Imber A.N., Maguire B.C., Laxmikanthan G., Schneider C.,
RA Gaffney B.J., Brash A.R.;
RT "On the relationships of substrate orientation, hydrogen abstraction, and
RT product stereochemistry in single and double dioxygenations by soybean
RT lipoxygenase-1 and its Ala542Gly mutant.";
RL J. Biol. Chem. 280:38756-38766(2005).
RN [9]
RP CATALYTIC ACTIVITY.
RX PubMed=19324874; DOI=10.1074/jbc.m809014200;
RA Dangi B., Obeng M., Nauroth J.M., Teymourlouei M., Needham M., Raman K.,
RA Arterburn L.M.;
RT "Biogenic synthesis, purification, and chemical characterization of anti-
RT inflammatory resolvins derived from docosapentaenoic acid (DPAn-6).";
RL J. Biol. Chem. 284:14744-14759(2009).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH IRON IONS.
RX PubMed=8502991; DOI=10.1126/science.8502991;
RA Boyington J.C., Gaffney B.J., Amzel L.M.;
RT "The three-dimensional structure of an arachidonic acid 15-lipoxygenase.";
RL Science 260:1482-1486(1993).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH IRON IONS.
RX PubMed=8718858; DOI=10.1021/bi960576u;
RA Minor W., Steczko J., Stec B., Otwinowski Z., Bolin J.T., Walter R.,
RA Axelrod B.;
RT "Crystal structure of soybean lipoxygenase L-1 at 1.4-A resolution.";
RL Biochemistry 35:10687-10701(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-495 AND
RP GLN-697 IN COMPLEX WITH IRON IONS, AND MUTAGENESIS OF GLN-495 AND GLN-697.
RX PubMed=11412104; DOI=10.1021/bi002893d;
RA Tomchick D.R., Phan P., Cymborowski M., Minor W., Holman T.R.;
RT "Structural and functional characterization of second-coordination sphere
RT mutants of soybean lipoxygenase-1.";
RL Biochemistry 40:7509-7517(2001).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH IRON IONS, AND
RP MUTAGENESIS OF ASN-694.
RX PubMed=16922498; DOI=10.1021/bi060577e;
RA Segraves E.N., Chruszcz M., Neidig M.L., Ruddat V., Zhou J., Wecksler A.T.,
RA Minor W., Solomon E.I., Holman T.R.;
RT "Kinetic, spectroscopic, and structural investigations of the soybean
RT lipoxygenase-1 first-coordination sphere mutant, Asn694Gly.";
RL Biochemistry 45:10233-10242(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON IONS.
RX PubMed=18441029; DOI=10.1529/biophysj.108.131789;
RA Chruszcz M., Wlodawer A., Minor W.;
RT "Determination of protein structures--a series of fortunate events.";
RL Biophys. J. 95:1-9(2008).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH IRON IONS, AND
RP MUTAGENESIS OF ILE-553.
RX PubMed=18216254; DOI=10.1073/pnas.0710643105;
RA Meyer M.P., Tomchick D.R., Klinman J.P.;
RT "Enzyme structure and dynamics affect hydrogen tunneling: the impact of a
RT remote side chain (I553) in soybean lipoxygenase-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:1146-1151(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH IRON IONS, AND
RP MUTAGENESIS OF LEU-546 AND LEU-754.
RX PubMed=24884374; DOI=10.1021/ja502726s;
RA Hu S., Sharma S.C., Scouras A.D., Soudackov A.V., Carr C.A.,
RA Hammes-Schiffer S., Alber T., Klinman J.P.;
RT "Extremely elevated room-temperature kinetic isotope effects quantify the
RT critical role of barrier width in enzymatic C-H activation.";
RL J. Am. Chem. Soc. 136:8157-8160(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
RX PubMed=28691068; DOI=10.1021/acscentsci.7b00142;
RA Offenbacher A.R., Hu S., Poss E.M., Carr C.A.M., Scouras A.D.,
RA Prigozhin D.M., Iavarone A.T., Palla A., Alber T., Fraser J.S.,
RA Klinman J.P.;
RT "Hydrogen-deuterium exchange of lipoxygenase uncovers a relationship
RT between distal, solvent exposed protein motions and the thermal activation
RT barrier for catalytic proton-coupled electron tunneling.";
RL ACS Cent. Sci. 3:570-579(2017).
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding. With linoleate as
CC substrate, L-1 shows a preference for carbon 13 as the site for
CC hydroperoxidation (in contrast to L-2 and L-3, which utilize either
CC carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-
CC hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases,
CC the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0
CC it represents about 25 % of the products.
CC {ECO:0000269|PubMed:16157595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (13S)-hydroperoxy-(9Z,11E)-
CC octadecadienoate; Xref=Rhea:RHEA:22780, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:57466; EC=1.13.11.12;
CC Evidence={ECO:0000269|PubMed:16157595, ECO:0000269|PubMed:2492826};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + O2 = (13S)-hydroperoxy-
CC (9Z,11E,15Z)-octadecatrienoate; Xref=Rhea:RHEA:34495,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32387, ChEBI:CHEBI:58757;
CC EC=1.13.11.12; Evidence={ECO:0000269|PubMed:16157595,
CC ECO:0000269|PubMed:2492826};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = (17S)-
CC hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate;
CC Xref=Rhea:RHEA:50840, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:133795; Evidence={ECO:0000269|PubMed:19324874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50841;
CC Evidence={ECO:0000269|PubMed:19324874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z)-docosapentaenoate + O2 = (17S)-
CC hydroperoxy-(4Z,7Z,10Z,13Z,15E)-docosapentaenoate;
CC Xref=Rhea:RHEA:50828, ChEBI:CHEBI:15379, ChEBI:CHEBI:77226,
CC ChEBI:CHEBI:133796; Evidence={ECO:0000269|PubMed:19324874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50829;
CC Evidence={ECO:0000269|PubMed:19324874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 = 17-hydroperoxy-
CC (7Z,10Z,13Z,15E,19Z)-docosapentaenoate; Xref=Rhea:RHEA:50832,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:77224, ChEBI:CHEBI:133797;
CC Evidence={ECO:0000269|PubMed:19324874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50833;
CC Evidence={ECO:0000269|PubMed:19324874};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726,
CC ECO:0000269|PubMed:8518276};
CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726, ECO:0000269|PubMed:8518276};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Inactive below pH 6.0. {ECO:0000269|PubMed:2492826};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11412104,
CC ECO:0000269|PubMed:8502991, ECO:0000269|PubMed:8718858}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: The hydroperoxide product serves to activate the resting
CC enzyme. The activation is accompanied by the oxidation of
CC Fe(2+)entadiene structure. L-1 prefers anionic substrate.
CC -!- MISCELLANEOUS: Soybean contains at least 4 distinct isoenzymes, L-1, L-
CC 2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in
CC the hypocotyl/radicle region of the seedling stem.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA47717.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J02795; AAA33986.1; -; mRNA.
DR EMBL; X67304; CAA47717.1; ALT_FRAME; mRNA.
DR PIR; S25064; DASYL2.
DR RefSeq; NP_001236153.1; NM_001249224.1.
DR PDB; 1F8N; X-ray; 1.40 A; A=1-839.
DR PDB; 1FGM; X-ray; 1.90 A; A=1-839.
DR PDB; 1FGO; X-ray; 1.62 A; A=1-839.
DR PDB; 1FGQ; X-ray; 1.85 A; A=1-839.
DR PDB; 1FGR; X-ray; 1.60 A; A=1-839.
DR PDB; 1FGT; X-ray; 1.62 A; A=1-839.
DR PDB; 1Y4K; X-ray; 1.95 A; A=1-839.
DR PDB; 1YGE; X-ray; 1.40 A; A=1-839.
DR PDB; 2SBL; X-ray; 2.60 A; A/B=1-839.
DR PDB; 3BNB; X-ray; 1.45 A; A=1-839.
DR PDB; 3BNC; X-ray; 1.65 A; A=1-839.
DR PDB; 3BND; X-ray; 1.60 A; A=1-839.
DR PDB; 3BNE; X-ray; 1.40 A; A=1-839.
DR PDB; 3PZW; X-ray; 1.40 A; A=1-839.
DR PDB; 4WFO; X-ray; 1.14 A; A=1-839.
DR PDB; 4WHA; X-ray; 1.70 A; A=1-839.
DR PDB; 5EEO; X-ray; 2.10 A; A=1-839.
DR PDB; 5T5V; X-ray; 1.80 A; A/B=1-839.
DR PDB; 5TQN; X-ray; 1.80 A; A/B=1-839.
DR PDB; 5TQO; X-ray; 1.70 A; A/B=1-839.
DR PDB; 5TQP; X-ray; 1.70 A; A/B=1-839.
DR PDB; 5TR0; X-ray; 1.85 A; A/B=1-839.
DR PDBsum; 1F8N; -.
DR PDBsum; 1FGM; -.
DR PDBsum; 1FGO; -.
DR PDBsum; 1FGQ; -.
DR PDBsum; 1FGR; -.
DR PDBsum; 1FGT; -.
DR PDBsum; 1Y4K; -.
DR PDBsum; 1YGE; -.
DR PDBsum; 2SBL; -.
DR PDBsum; 3BNB; -.
DR PDBsum; 3BNC; -.
DR PDBsum; 3BND; -.
DR PDBsum; 3BNE; -.
DR PDBsum; 3PZW; -.
DR PDBsum; 4WFO; -.
DR PDBsum; 4WHA; -.
DR PDBsum; 5EEO; -.
DR PDBsum; 5T5V; -.
DR PDBsum; 5TQN; -.
DR PDBsum; 5TQO; -.
DR PDBsum; 5TQP; -.
DR PDBsum; 5TR0; -.
DR AlphaFoldDB; P08170; -.
DR SMR; P08170; -.
DR STRING; 3847.GLYMA13G42320.1; -.
DR BindingDB; P08170; -.
DR ChEMBL; CHEMBL4586; -.
DR DrugCentral; P08170; -.
DR SwissLipids; SLP:000001639; -.
DR PRIDE; P08170; -.
DR GeneID; 547923; -.
DR KEGG; gmx:547923; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; P08170; -.
DR OrthoDB; 385042at2759; -.
DR SABIO-RK; P08170; -.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; P08170; -.
DR PRO; PR:P08170; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0016165; F:linoleate 13S-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0102299; F:linolenate 9R-lipoxygenase activity; IDA:UniProtKB.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:UniProtKB.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dioxygenase; Direct protein sequencing;
KW Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis;
KW Lipid metabolism; Metal-binding; Oxidoreductase; Oxylipin biosynthesis;
KW Reference proteome.
FT CHAIN 1..839
FT /note="Seed linoleate 13S-lipoxygenase-1"
FT /id="PRO_0000220717"
FT DOMAIN 16..145
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 148..839
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 212..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 499
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726,
FT ECO:0000269|PubMed:8502991, ECO:0007744|PDB:2SBL"
FT BINDING 504
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726,
FT ECO:0000269|PubMed:8502991, ECO:0007744|PDB:2SBL"
FT BINDING 690
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726,
FT ECO:0000269|PubMed:8502991, ECO:0007744|PDB:2SBL"
FT BINDING 694
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726,
FT ECO:0000269|PubMed:8502991, ECO:0007744|PDB:2SBL"
FT BINDING 839
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:8502991,
FT ECO:0007744|PDB:2SBL"
FT MUTAGEN 494
FT /note="H->Q: 37% of wild-type activity."
FT MUTAGEN 494
FT /note="H->S: 8% of wild-type activity."
FT MUTAGEN 495
FT /note="Q->A: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:11412104"
FT MUTAGEN 495
FT /note="Q->E: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:11412104"
FT MUTAGEN 499
FT /note="H->Q: Inactive."
FT MUTAGEN 504
FT /note="H->Q,S: Inactive."
FT MUTAGEN 517
FT /note="H->Q: 33% of wild-type activity."
FT MUTAGEN 522
FT /note="H->Q: 1% of wild-type activity."
FT MUTAGEN 531
FT /note="H->Q: 20% of wild-type activity."
FT MUTAGEN 542
FT /note="A->G: Changes reaction profile to produce almost
FT equal amounts of 13S- and 9R-hydroperoxyoctadecadienoate."
FT /evidence="ECO:0000269|PubMed:16157595"
FT MUTAGEN 542
FT /note="A->S: Little effect on reaction profile."
FT /evidence="ECO:0000269|PubMed:16157595"
FT MUTAGEN 542
FT /note="A->T,V: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:16157595"
FT MUTAGEN 546
FT /note="L->A: Reduces catalytic efficiency more than 14000-
FT fold; when associated with A-754."
FT /evidence="ECO:0000269|PubMed:24884374"
FT MUTAGEN 553
FT /note="I->G: Reduces catalytic efficiency 230-fold."
FT /evidence="ECO:0000269|PubMed:18216254"
FT MUTAGEN 690
FT /note="H->Q: Inactive."
FT MUTAGEN 694
FT /note="N->G: Reduces catalytic efficiency 5-fold."
FT /evidence="ECO:0000269|PubMed:16922498"
FT MUTAGEN 697
FT /note="Q->N,E: Reduces catalytic activity."
FT /evidence="ECO:0000269|PubMed:11412104"
FT MUTAGEN 754
FT /note="L->A: Reduces catalytic efficiency more than 14000-
FT fold; when associated with A-546."
FT /evidence="ECO:0000269|PubMed:24884374"
FT CONFLICT 426..427
FT /note="AK -> RN (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 558..560
FT /note="LPS -> AL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 572..574
FT /note="KNW -> EL (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 641
FT /note="N -> P (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 741..748
FT /note="KLPTLISL -> SCRLSLAV (in Ref. 3)"
FT /evidence="ECO:0000305"
FT STRAND 7..16
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:1YGE"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 39..50
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:4WFO"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 301..307
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1Y4K"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 343..352
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 395..400
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 410..421
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 473..496
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 497..503
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 504..517
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 535..545
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 552..556
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 563..571
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 576..579
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 581..587
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 600..605
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 609..628
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 636..640
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 643..654
FT /evidence="ECO:0007829|PDB:4WFO"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 669..671
FT /evidence="ECO:0007829|PDB:1YGE"
FT HELIX 672..686
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 688..694
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 697..701
FT /evidence="ECO:0007829|PDB:4WFO"
FT TURN 704..706
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 718..720
FT /evidence="ECO:0007829|PDB:5TR0"
FT HELIX 721..728
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 730..737
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 741..754
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 776..801
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 803..805
FT /evidence="ECO:0007829|PDB:4WFO"
FT HELIX 806..809
FT /evidence="ECO:0007829|PDB:4WFO"
FT TURN 810..814
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:4WFO"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:4WFO"
SQ SEQUENCE 839 AA; 94369 MW; 1586250ACD3E34A4 CRC64;
MFSAGHKIKG TVVLMPKNEL EVNPDGSAVD NLNAFLGRSV SLQLISATKA DAHGKGKVGK
DTFLEGINTS LPTLGAGESA FNIHFEWDGS MGIPGAFYIK NYMQVEFFLK SLTLEAISNQ
GTIRFVCNSW VYNTKLYKSV RIFFANHTYV PSETPAPLVS YREEELKSLR GNGTGERKEY
DRIYDYDVYN DLGNPDKSEK LARPVLGGSS TFPYPRRGRT GRGPTVTDPN TEKQGEVFYV
PRDENLGHLK SKDALEIGTK SLSQIVQPAF ESAFDLKSTP IEFHSFQDVH DLYEGGIKLP
RDVISTIIPL PVIKELYRTD GQHILKFPQP HVVQVSQSAW MTDEEFAREM IAGVNPCVIR
GLEEFPPKSN LDPAIYGDQS SKITADSLDL DGYTMDEALG SRRLFMLDYH DIFMPYVRQI
NQLNSAKTYA TRTILFLRED GTLKPVAIEL SLPHSAGDLS AAVSQVVLPA KEGVESTIWL
LAKAYVIVND SCYHQLMSHW LNTHAAMEPF VIATHRHLSV LHPIYKLLTP HYRNNMNINA
LARQSLINAN GIIETTFLPS KYSVEMSSAV YKNWVFTDQA LPADLIKRGV AIKDPSTPHG
VRLLIEDYPY AADGLEIWAA IKTWVQEYVP LYYARDDDVK NDSELQHWWK EAVEKGHGDL
KDKPWWPKLQ TLEDLVEVCL IIIWIASALH AAVNFGQYPY GGLIMNRPTA SRRLLPEKGT
PEYEEMINNH EKAYLRTITS KLPTLISLSV IEILSTHASD EVYLGQRDNP HWTSDSKALQ
AFQKFGNKLK EIEEKLVRRN NDPSLQGNRL GPVQLPYTLL YPSSEEGLTF RGIPNSISI
