LOX_AERVM
ID LOX_AERVM Reviewed; 374 AA.
AC Q44467;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=L-lactate oxidase {ECO:0000303|PubMed:17142893, ECO:0000303|PubMed:17517371, ECO:0000303|PubMed:18367206, ECO:0000303|PubMed:27302031, ECO:0000303|PubMed:8589073, ECO:0000303|Ref.1};
DE Short=LOD {ECO:0000303|Ref.1};
DE Short=LOX {ECO:0000303|PubMed:17142893, ECO:0000303|PubMed:17517371, ECO:0000303|PubMed:18367206, ECO:0000303|PubMed:27302031};
DE EC=1.1.3.- {ECO:0000269|PubMed:25423902, ECO:0000269|PubMed:26260739, ECO:0000269|PubMed:27302031, ECO:0000269|PubMed:2818595, ECO:0000269|PubMed:8589073, ECO:0000269|Ref.1};
DE AltName: Full=Lactate oxidase {ECO:0000303|PubMed:18367206, ECO:0000303|PubMed:27302031, ECO:0000303|PubMed:2818595, ECO:0000303|Ref.1};
OS Aerococcus viridans (strain ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461
OS / NBRC 12219 / NCTC 8251 / M1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus.
OX NCBI_TaxID=655812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 1-7, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC
RC 8251 / M1;
RX DOI=10.1007/BF00127437;
RA Minagawa H., Nakayama N., Nakamoto S.;
RT "Thermostabilization of lactate oxidase by random mutagenesis.";
RL Biotechnol. Lett. 17:975-980(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, SUBUNIT, AND
RP ACTIVITY REGULATION.
RC STRAIN=ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC
RC 8251 / M1;
RX PubMed=2818595; DOI=10.1016/0006-291x(89)91546-5;
RA Duncan J.D., Wallis J.O., Azari M.R.;
RT "Purification and properties of Aerococcus viridans lactate oxidase.";
RL Biochem. Biophys. Res. Commun. 164:919-926(1989).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 11563 / DSM 20340 / CCUG 4311 / JCM 20461 / NBRC 12219 / NCTC
RC 8251 / M1;
RX PubMed=8589073; DOI=10.1016/0300-9084(96)88178-8;
RA Maeda-Yorita K., Aki K., Sagai H., Misaki H., Massey V.;
RT "L-lactate oxidase and L-lactate monooxygenase: mechanistic variations on a
RT common structural theme.";
RL Biochimie 77:631-642(1995).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=20518470; DOI=10.1021/ac1004426;
RA Romero M.R., Ahumada F., Garay F., Baruzzi A.M.;
RT "Amperometric biosensor for direct blood lactate detection.";
RL Anal. Chem. 82:5568-5572(2010).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=31999581; DOI=10.1016/j.bios.2019.111974;
RA Hiraka K., Kojima K., Tsugawa W., Asano R., Ikebukuro K., Sode K.;
RT "Rational engineering of Aerococcus viridans L-lactate oxidase for the
RT mediator modification to achieve quasi-direct electron transfer type
RT lactate sensor.";
RL Biosens. Bioelectron. 151:111974-111974(2020).
RN [6] {ECO:0007744|PDB:2J6X}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FMN, AND COFACTOR.
RX PubMed=17142893; DOI=10.1107/s1744309106044678;
RA Leiros I., Wang E., Rasmussen T., Oksanen E., Repo H., Petersen S.B.,
RA Heikinheimo P., Hough E.;
RT "The 2.1 A structure of Aerococcus viridans L-lactate oxidase (LOX).";
RL Acta Crystallogr. F Struct. Biol. Commun. 62:1185-1190(2006).
RN [7] {ECO:0007744|PDB:2DU2}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FMN, AND COFACTOR.
RX PubMed=17007814; DOI=10.1016/j.bbrc.2006.09.025;
RA Umena Y., Yorita K., Matsuoka T., Kita A., Fukui K., Morimoto Y.;
RT "The crystal structure of L-lactate oxidase from Aerococcus viridans at
RT 2.1A resolution reveals the mechanism of strict substrate recognition.";
RL Biochem. Biophys. Res. Commun. 350:249-256(2006).
RN [8] {ECO:0007744|PDB:2E77}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FMN AND PYRUVATE,
RP AND COFACTOR.
RX PubMed=17517371; DOI=10.1016/j.bbrc.2007.05.021;
RA Li S.J., Umena Y., Yorita K., Matsuoka T., Kita A., Fukui K., Morimoto Y.;
RT "Crystallographic study on the interaction of L-lactate oxidase with
RT pyruvate at 1.9 Angstrom resolution.";
RL Biochem. Biophys. Res. Commun. 358:1002-1007(2007).
RN [9] {ECO:0007744|PDB:2NLI, ECO:0007744|PDB:2ZFA}
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 7-374 IN COMPLEXES WITH FMN AND
RP D-LACTATE, AND COFACTOR.
RX PubMed=18367206; DOI=10.1016/j.jmb.2008.02.062;
RA Furuichi M., Suzuki N., Dhakshnamoorhty B., Minagawa H., Yamagishi R.,
RA Watanabe Y., Goto Y., Kaneko H., Yoshida Y., Yagi H., Waga I., Kumar P.K.,
RA Mizuno H.;
RT "X-ray structures of Aerococcus viridans lactate oxidase and its complex
RT with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism.";
RL J. Mol. Biol. 378:436-446(2008).
RN [10] {ECO:0007744|PDB:4RJE}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF MUTANT GLY-95 IN COMPLEX WITH FMN
RP AND PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ALA-95.
RX PubMed=25423902; DOI=10.1111/febs.13162;
RA Stoisser T., Rainer D., Leitgeb S., Wilson D.K., Nidetzky B.;
RT "The Ala95-to-Gly substitution in Aerococcus viridans L-lactate oxidase
RT revisited - structural consequences at the catalytic site and effect on
RT reactivity with O2 and other electron acceptors.";
RL FEBS J. 282:562-578(2015).
RN [11] {ECO:0007744|PDB:4YL2}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT PHE-191 IN COMPLEX WITH
RP FMN AND PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND MUTAGENESIS OF TYR-191.
RX PubMed=26260739; DOI=10.1111/febs.13409;
RA Stoisser T., Klimacek M., Wilson D.K., Nidetzky B.;
RT "Speeding up the product release: a second-sphere contribution from Tyr191
RT to the reactivity of L-lactate oxidase revealed in crystallographic and
RT kinetic studies of site-directed variants.";
RL FEBS J. 282:4130-4140(2015).
RN [12] {ECO:0007744|PDB:5EBU}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT PHE-215 IN COMPLEX WITH
RP FMN AND PYRUVATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, AND MUTAGENESIS OF TYR-215.
RX PubMed=27302031; DOI=10.1038/srep27892;
RA Stoisser T., Brunsteiner M., Wilson D.K., Nidetzky B.;
RT "Conformational flexibility related to enzyme activity: evidence for a
RT dynamic active-site gatekeeper function of Tyr(215) in Aerococcus viridans
RT lactate oxidase.";
RL Sci. Rep. 6:27892-27892(2016).
CC -!- FUNCTION: Catalyzes the oxidation of (S)-lactate (L-lactate) to
CC pyruvate, with a reduction of O2 to H2O2 (Ref.1, PubMed:27302031,
CC PubMed:25423902, PubMed:2818595, PubMed:8589073, PubMed:26260739).
CC Cannot oxidize D-lactate, glycolate, and D,L-2-hydroxybutanoate
CC (PubMed:2818595). May be involved in the utilization of L-lactate as an
CC energy source for growth (By similarity).
CC {ECO:0000250|UniProtKB:O33655, ECO:0000269|PubMed:25423902,
CC ECO:0000269|PubMed:26260739, ECO:0000269|PubMed:27302031,
CC ECO:0000269|PubMed:2818595, ECO:0000269|PubMed:8589073,
CC ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactate + O2 = H2O2 + pyruvate; Xref=Rhea:RHEA:55868,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16651; Evidence={ECO:0000269|PubMed:25423902,
CC ECO:0000269|PubMed:26260739, ECO:0000269|PubMed:27302031,
CC ECO:0000269|PubMed:2818595, ECO:0000269|PubMed:8589073,
CC ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55869;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:17007814, ECO:0000269|PubMed:17142893,
CC ECO:0000269|PubMed:17517371, ECO:0000269|PubMed:18367206,
CC ECO:0000269|PubMed:25423902, ECO:0000269|PubMed:26260739,
CC ECO:0000269|PubMed:27302031, ECO:0000269|PubMed:2818595,
CC ECO:0000269|PubMed:8589073};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:17007814,
CC ECO:0000269|PubMed:17142893, ECO:0000269|PubMed:17517371,
CC ECO:0000269|PubMed:18367206, ECO:0000269|PubMed:25423902,
CC ECO:0000269|PubMed:26260739, ECO:0000269|PubMed:27302031};
CC -!- ACTIVITY REGULATION: L-lactate oxidation is competitively inhibited by
CC glycolate, D-lactate, oxalate and 2-hydroxybutanoate.
CC {ECO:0000269|PubMed:2818595}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for (S)-lactate {ECO:0000269|Ref.1};
CC KM=0.43 mM for (S)-lactate {ECO:0000269|PubMed:2818595};
CC KM=0.94 mM for (S)-lactate (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:8589073};
CC KM=0.16 mM for O2 (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:8589073};
CC KM=0.50 mM for (S)-lactate (at pH 6.5 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:26260739, ECO:0000269|PubMed:27302031};
CC KM=51 uM for O2 (at pH 6.5 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:27302031};
CC Note=kcat is 88 sec(-1) for (S)-lactate oxidation (at pH 6.5 and 20
CC degrees Celsius) (PubMed:27302031, PubMed:26260739). kcat is 220
CC sec(-1) for (S)-lactate oxidation (at pH 7 and 25 degrees Celsius)
CC (PubMed:8589073). {ECO:0000269|PubMed:26260739,
CC ECO:0000269|PubMed:27302031, ECO:0000269|PubMed:8589073};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius. {ECO:0000269|Ref.1};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:2818595, ECO:0000269|Ref.1}.
CC -!- BIOTECHNOLOGY: Is widely used in biosensors to measure the lactate
CC concentration in blood and other tissues. {ECO:0000269|PubMed:20518470,
CC ECO:0000269|PubMed:31999581}.
CC -!- MISCELLANEOUS: The proposed reaction pathway consists of two half-
CC reactions, in which FMN is first reduced by L-lactate to become
CC subsequently reoxidized by O2. {ECO:0000269|PubMed:27302031}.
CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; D50611; BAA09172.1; -; Genomic_DNA.
DR PIR; I39549; I39549.
DR PDB; 2DU2; X-ray; 2.10 A; A/B/C/D=1-374.
DR PDB; 2E77; X-ray; 1.90 A; A/B/C/D=1-374.
DR PDB; 2J6X; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-374.
DR PDB; 2NLI; X-ray; 1.59 A; A/B=7-374.
DR PDB; 2ZFA; X-ray; 1.81 A; A/B=1-374.
DR PDB; 4RJE; X-ray; 1.65 A; A/B/C/D=1-374.
DR PDB; 4YL2; X-ray; 1.90 A; A/B/C/D=1-374.
DR PDB; 5EBU; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-374.
DR PDBsum; 2DU2; -.
DR PDBsum; 2E77; -.
DR PDBsum; 2J6X; -.
DR PDBsum; 2NLI; -.
DR PDBsum; 2ZFA; -.
DR PDBsum; 4RJE; -.
DR PDBsum; 4YL2; -.
DR PDBsum; 5EBU; -.
DR SMR; Q44467; -.
DR BRENDA; 1.1.1.27; 161.
DR BRENDA; 1.1.3.2; 161.
DR EvolutionaryTrace; Q44467; -.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR InterPro; IPR000262; FMN-dep_DH.
DR InterPro; IPR037396; FMN_HAD.
DR InterPro; IPR008259; FMN_hydac_DH_AS.
DR InterPro; IPR014080; L_lactate_ox.
DR Pfam; PF01070; FMN_dh; 1.
DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR TIGRFAMs; TIGR02708; L_lactate_ox; 1.
DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; Metal-binding;
KW Nucleotide-binding; Oxidoreductase; Pyruvate.
FT CHAIN 1..374
FT /note="L-lactate oxidase"
FT /id="PRO_0000454869"
FT DOMAIN 14..370
FT /note="FMN hydroxy acid dehydrogenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00683"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27302031"
FT BINDING 40
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:4RJE"
FT BINDING 93..95
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2DU2,
FT ECO:0007744|PDB:2E77, ECO:0007744|PDB:2NLI"
FT BINDING 122
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:2NLI"
FT BINDING 144
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0007744|PDB:2E77"
FT BINDING 146
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:4RJE"
FT BINDING 172
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:2NLI"
FT BINDING 181
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:4RJE"
FT BINDING 215
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:4RJE"
FT BINDING 241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:2NLI"
FT BINDING 263
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:2NLI"
FT BINDING 265
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:4RJE"
FT BINDING 268
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:25423902, ECO:0007744|PDB:2E77,
FT ECO:0007744|PDB:4RJE"
FT BINDING 296..300
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2DU2,
FT ECO:0007744|PDB:2E77, ECO:0007744|PDB:2NLI"
FT BINDING 320
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:17517371,
FT ECO:0000269|PubMed:18367206, ECO:0007744|PDB:2DU2,
FT ECO:0007744|PDB:2E77, ECO:0007744|PDB:2NLI"
FT SITE 215
FT /note="Is suggested to participate in control of
FT opening/closing motions of the active-site lid in
FT A.viridans LOX"
FT /evidence="ECO:0000305|PubMed:27302031"
FT MUTAGEN 95
FT /note="A->G: The mutant is three-fold more reactive towards
FT DCIP than O2 as the electron acceptor, whereas wild-type
FT under the same conditions is 14-fold more reactive towards
FT O2 than DCIP. Substituted 1,4-benzoquinones are up to five-
FT fold better electron acceptors for reaction with this
FT mutant than wild-type."
FT /evidence="ECO:0000269|PubMed:25423902"
FT MUTAGEN 191
FT /note="Y->A: 18-fold decrease in activity and 92-fold
FT decrease in affinity for (L)-lactate."
FT /evidence="ECO:0000269|PubMed:26260739"
FT MUTAGEN 191
FT /note="Y->F: 4-fold decrease in activity and 6-fold
FT increase in affinity for (L)-lactate."
FT /evidence="ECO:0000269|PubMed:26260739"
FT MUTAGEN 191
FT /note="Y->L: 12-fold decrease in activity and 3-fold
FT decrease in affinity for (L)-lactate."
FT /evidence="ECO:0000269|PubMed:26260739"
FT MUTAGEN 215
FT /note="Y->F: No significant change in catalytic efficiency,
FT with a 4-fold decrease in activity and a 4-fold increase in
FT affinity for (L)-lactate. Affects the pyruvate release
FT rate."
FT /evidence="ECO:0000269|PubMed:27302031"
FT MUTAGEN 215
FT /note="Y->H: 18-fold decrease in the catalytic efficiency.
FT The catalytic reduction of FMN is affected more strongly
FT (33-fold decrease) than the pyruvate release (5.4-fold
FT decrease)."
FT /evidence="ECO:0000269|PubMed:27302031"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 104..115
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:4RJE"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:4YL2"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:2NLI"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:2ZFA"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:4RJE"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:2NLI"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:4RJE"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 320..352
FT /evidence="ECO:0007829|PDB:2NLI"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:2NLI"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2NLI"
SQ SEQUENCE 374 AA; 40933 MW; 9D27951C901FDBE1 CRC64;
MNNNDIEYNA PSEIKYIDVV NTYDLEEEAS KVVPHGGFNY IAGASGDEWT KRANDRAWKH
KLLYPRLAQD VEAPDTSTEI LGHKIKAPFI MAPIAAHGLA HTTKEAGTAR AVSEFGTIMS
ISAYSGATFE EISEGLNGGP RWFQIYMAKD DQQNRDILDE AKSDGATAII LTADSTVSGN
RDRDVKNKFV YPFGMPIVQR YLRGTAEGMS LNNIYGASKQ KISPRDIEEI AGHSGLPVFV
KGIQHPEDAD MAIKRGASGI WVSNHGARQL YEAPGSFDTL PAIAERVNKR VPIVFDSGVR
RGEHVAKALA SGADVVALGR PVLFGLALGG WQGAYSVLDY FQKDLTRVMQ LTGSQNVEDL
KGLDLFDNPY GYEY
