TMOA_PSEME
ID TMOA_PSEME Reviewed; 500 AA.
AC Q00456; Q6Q8Q7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 3.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Toluene-4-monooxygenase system, hydroxylase component subunit alpha {ECO:0000303|PubMed:15240250};
DE Short=T4MO {ECO:0000303|PubMed:1885512};
DE EC=1.14.13.236 {ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873, ECO:0000305|PubMed:2019563};
DE AltName: Full=Toluene-4-monooxygenase hydroxylase subunit {ECO:0000303|PubMed:1885512};
DE Short=T4moH {ECO:0000303|PubMed:1885512};
DE AltName: Full=Toluene-4-monooxygenase system protein A {ECO:0000303|PubMed:1885512};
DE Short=T4moA {ECO:0000303|PubMed:1885512};
GN Name=tmoA {ECO:0000303|PubMed:1885512};
OS Pseudomonas mendocina.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=300;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-14, FUNCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=KR1;
RX PubMed=1885512; DOI=10.1128/jb.173.17.5315-5327.1991;
RA Yen K.-M., Karl M.R., Blatt L.M., Simon M.J., Winter R.B., Fausset P.R.,
RA Lu H.S., Harcourt A.A., Chen K.K.;
RT "Cloning and characterization of a Pseudomonas mendocina KR1 gene cluster
RT encoding toluene-4-monooxygenase.";
RL J. Bacteriol. 173:5315-5327(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=KR1 {ECO:0000312|EMBL:AAS66660.1};
RX PubMed=15240250; DOI=10.1128/aem.70.7.3814-3820.2004;
RA Tao Y., Fishman A., Bentley W.E., Wood T.K.;
RT "Oxidation of benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by
RT toluene 4-monooxygenase of Pseudomonas mendocina KR1 and toluene 3-
RT monooxygenase of Ralstonia pickettii PKO1.";
RL Appl. Environ. Microbiol. 70:3814-3820(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND COFACTOR.
RC STRAIN=KR1;
RX PubMed=2019563; DOI=10.1128/jb.173.9.3010-3016.1991;
RA Whited G.M., Gibson D.T.;
RT "Toluene-4-monooxygenase, a three-component enzyme system that catalyzes
RT the oxidation of toluene to p-cresol in Pseudomonas mendocina KR1.";
RL J. Bacteriol. 173:3010-3016(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH IRON, COFACTOR, AND
RP SUBUNIT.
RX PubMed=19033467; DOI=10.1073/pnas.0807948105;
RA Bailey L.J., McCoy J.G., Phillips G.N. Jr., Fox B.G.;
RT "Structural consequences of effector protein complex formation in a diiron
RT hydroxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19194-19198(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) IN COMPLEX WITH IRON, FUNCTION,
RP COFACTOR, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-201, AND SUBUNIT.
RX PubMed=19290655; DOI=10.1021/bi900144a;
RA Elsen N.L., Bailey L.J., Hauser A.D., Fox B.G.;
RT "Role for threonine 201 in the catalytic cycle of the soluble diiron
RT hydroxylase toluene 4-monooxygenase.";
RL Biochemistry 48:3838-3846(2009).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH IRON, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF GLY-103, AND SUBUNIT.
RX PubMed=19705873; DOI=10.1021/bi901150a;
RA Bailey L.J., Fox B.G.;
RT "Crystallographic and catalytic studies of the peroxide-shunt reaction in a
RT diiron hydroxylase.";
RL Biochemistry 48:8932-8939(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF WILD-TYPE AND MUTANT LEU-103 IN
RP COMPLEX WITH IRON, MUTAGENESIS OF GLY-103, COFACTOR, AND SUBUNIT.
RC STRAIN=KR1;
RX PubMed=22264099; DOI=10.1021/bi2018333;
RA Bailey L.J., Acheson J.F., McCoy J.G., Elsen N.L., Phillips G.N. Jr.,
RA Fox B.G.;
RT "Crystallographic analysis of active site contributions to regiospecificity
RT in the diiron enzyme toluene 4-monooxygenase.";
RL Biochemistry 51:1101-1113(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 2-491 IN COMPLEX WITH IRON,
RP COFACTOR, AND SUBUNIT.
RX PubMed=25248368; DOI=10.1038/ncomms6009;
RA Acheson J.F., Bailey L.J., Elsen N.L., Fox B.G.;
RT "Structural basis for biomolecular recognition in overlapping binding sites
RT in a diiron enzyme system.";
RL Nat. Commun. 5:5009-5009(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 1-493 OF WILD-TYPE AND MUTANT
RP ALA-228 IN COMPLEX WITH IRON, MUTAGENESIS OF GLN-228, COFACTOR, AND
RP SUBUNIT.
RX PubMed=28346937; DOI=10.1038/nature21681;
RA Acheson J.F., Bailey L.J., Brunold T.C., Fox B.G.;
RT "In-crystal reaction cycle of a toluene-bound diiron hydroxylase.";
RL Nature 544:191-195(2017).
CC -!- FUNCTION: Component of the toluene-4-monooxygenase multicomponent
CC enzyme system which catalyzes the O2- and NADH-dependent hydroxylation
CC of toluene to form p-cresol (PubMed:1885512, PubMed:15240250,
CC PubMed:2019563, PubMed:19290655, PubMed:19705873). Also able to convert
CC benzene to phenol, catechol, and 1,2,3-trihydroxybenzene by successive
CC hydroxylations (PubMed:15240250). {ECO:0000269|PubMed:15240250,
CC ECO:0000269|PubMed:1885512, ECO:0000269|PubMed:19290655,
CC ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:2019563}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + toluene = 4-methylphenol + H2O + NAD(+);
CC Xref=Rhea:RHEA:41380, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:17578, ChEBI:CHEBI:17847,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.14.13.236;
CC Evidence={ECO:0000269|PubMed:15240250, ECO:0000269|PubMed:19290655,
CC ECO:0000269|PubMed:19705873, ECO:0000305|PubMed:2019563};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:19033467, ECO:0000269|PubMed:19290655,
CC ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:22264099,
CC ECO:0000269|PubMed:25248368, ECO:0000269|PubMed:28346937,
CC ECO:0000305|PubMed:2019563};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000269|PubMed:19033467,
CC ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
CC ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
CC ECO:0000269|PubMed:28346937};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+) and Cu(2+).
CC {ECO:0000269|PubMed:2019563}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:2019563};
CC -!- PATHWAY: Xenobiotic degradation; toluene degradation.
CC {ECO:0000305|PubMed:15240250}.
CC -!- SUBUNIT: The alkene monooxygenase multicomponent enzyme system is
CC composed of an electron transfer component and a monooxygenase
CC component interacting with the effector protein TmoD. The electron
CC transfer component is composed of a ferredoxin reductase (TmoF) and a
CC ferredoxin (TmoC), and the monooxygenase component is formed by a
CC heterohexamer (dimer of heterotrimers) of two alpha subunits (TmoA),
CC two beta subunits (TmoE) and two gamma subunits (TmoB).
CC {ECO:0000269|PubMed:19033467, ECO:0000269|PubMed:19290655,
CC ECO:0000269|PubMed:19705873, ECO:0000269|PubMed:22264099,
CC ECO:0000269|PubMed:25248368, ECO:0000269|PubMed:28346937}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a complete loss of
CC toluene-4-monooxygenase activity. {ECO:0000269|PubMed:1885512}.
CC -!- SIMILARITY: Belongs to the TmoA/XamoA family. {ECO:0000305}.
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DR EMBL; M65106; AAA25999.1; -; Genomic_DNA.
DR EMBL; AY552601; AAS66660.1; -; Genomic_DNA.
DR PDB; 3DHG; X-ray; 1.85 A; A/D=1-500.
DR PDB; 3DHH; X-ray; 1.94 A; A=1-500.
DR PDB; 3DHI; X-ray; 1.68 A; A=1-500.
DR PDB; 3GE3; X-ray; 1.52 A; A=1-500.
DR PDB; 3GE8; X-ray; 2.19 A; A/D=1-500.
DR PDB; 3I5J; X-ray; 1.90 A; A=1-500.
DR PDB; 3I63; X-ray; 2.09 A; A=1-500.
DR PDB; 3Q14; X-ray; 1.75 A; A=1-500.
DR PDB; 3Q2A; X-ray; 1.99 A; A=1-500.
DR PDB; 3Q3M; X-ray; 1.75 A; A/D=1-500.
DR PDB; 3Q3N; X-ray; 1.84 A; A=1-500.
DR PDB; 3Q3O; X-ray; 1.95 A; A=1-500.
DR PDB; 3RI7; X-ray; 2.10 A; A=2-493.
DR PDB; 3RMK; X-ray; 1.95 A; A/D=2-493.
DR PDB; 4P1B; X-ray; 2.05 A; A/D=2-491.
DR PDB; 4P1C; X-ray; 2.40 A; A/D=2-491.
DR PDB; 5TDS; X-ray; 1.72 A; A/D=1-493.
DR PDB; 5TDT; X-ray; 1.82 A; A/D=1-493.
DR PDB; 5TDU; X-ray; 1.74 A; A=1-493.
DR PDB; 5TDV; X-ray; 2.00 A; A/D=1-500.
DR PDBsum; 3DHG; -.
DR PDBsum; 3DHH; -.
DR PDBsum; 3DHI; -.
DR PDBsum; 3GE3; -.
DR PDBsum; 3GE8; -.
DR PDBsum; 3I5J; -.
DR PDBsum; 3I63; -.
DR PDBsum; 3Q14; -.
DR PDBsum; 3Q2A; -.
DR PDBsum; 3Q3M; -.
DR PDBsum; 3Q3N; -.
DR PDBsum; 3Q3O; -.
DR PDBsum; 3RI7; -.
DR PDBsum; 3RMK; -.
DR PDBsum; 4P1B; -.
DR PDBsum; 4P1C; -.
DR PDBsum; 5TDS; -.
DR PDBsum; 5TDT; -.
DR PDBsum; 5TDU; -.
DR PDBsum; 5TDV; -.
DR AlphaFoldDB; Q00456; -.
DR SMR; Q00456; -.
DR DIP; DIP-48644N; -.
DR IntAct; Q00456; 3.
DR KEGG; ag:AAA25999; -.
DR BioCyc; MetaCyc:MON-2506; -.
DR BRENDA; 1.14.13.236; 31258.
DR UniPathway; UPA00273; -.
DR EvolutionaryTrace; Q00456; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0042203; P:toluene catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR003430; Phenol_Hydrox.
DR InterPro; IPR012348; RNR-like.
DR Pfam; PF02332; Phenol_Hydrox; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Iron; Metal-binding; Monooxygenase; NAD; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1885512"
FT CHAIN 2..500
FT /note="Toluene-4-monooxygenase system, hydroxylase
FT component subunit alpha"
FT /id="PRO_0000072599"
FT BINDING 104
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
FT ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14,
FT ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M,
FT ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O,
FT ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C,
FT ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT,
FT ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
FT ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14,
FT ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M,
FT ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O,
FT ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C,
FT ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT,
FT ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
FT ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14,
FT ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M,
FT ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O,
FT ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C,
FT ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT,
FT ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
FT ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14,
FT ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M,
FT ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O,
FT ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C,
FT ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT,
FT ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV"
FT BINDING 197
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
FT ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14,
FT ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M,
FT ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O,
FT ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C,
FT ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT,
FT ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0007744|PDB:3DHI"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
FT ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14,
FT ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M,
FT ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O,
FT ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C,
FT ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT,
FT ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:19033467,
FT ECO:0000269|PubMed:19290655, ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099, ECO:0000269|PubMed:25248368,
FT ECO:0000269|PubMed:28346937, ECO:0007744|PDB:3Q14,
FT ECO:0007744|PDB:3Q2A, ECO:0007744|PDB:3Q3M,
FT ECO:0007744|PDB:3Q3N, ECO:0007744|PDB:3Q3O,
FT ECO:0007744|PDB:3RI7, ECO:0007744|PDB:3RMK,
FT ECO:0007744|PDB:4P1B, ECO:0007744|PDB:4P1C,
FT ECO:0007744|PDB:5TDS, ECO:0007744|PDB:5TDT,
FT ECO:0007744|PDB:5TDU, ECO:0007744|PDB:5TDV"
FT MUTAGEN 103
FT /note="G->L: Increases production of m-cresol, instread of
FT p-cresol."
FT /evidence="ECO:0000269|PubMed:19705873,
FT ECO:0000269|PubMed:22264099"
FT MUTAGEN 201
FT /note="T->A: Strongly increases consumption of dioxygen in
FT the absence of bound substrate."
FT /evidence="ECO:0000269|PubMed:19290655"
FT MUTAGEN 228
FT /note="Q->A: Shows a strong decrease in the catalytic
FT efficiency for hydroxylation and only a minor change in the
FT affinity for toluene."
FT /evidence="ECO:0000269|PubMed:28346937"
FT CONFLICT 336..337
FT /note="WY -> LD (in Ref. 1; AAA25999)"
FT /evidence="ECO:0000305"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 55..76
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5TDS"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 87..117
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 121..146
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 147..151
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 193..199
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 218..234
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 251..278
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 317..337
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3DHI"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 424..430
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:3GE3"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 464..470
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:3GE3"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:3GE3"
FT HELIX 487..491
FT /evidence="ECO:0007829|PDB:3GE3"
SQ SEQUENCE 500 AA; 58104 MW; 39611B1A749C27E0 CRC64;
MAMHPRKDWY ELTRATNWTP SYVTEEQLFP ERMSGHMGIP LEKWESYDEP YKTSYPEYVS
IQREKDAGAY SVKAALERAK IYENSDPGWI STLKSHYGAI AVGEYAAVTG EGRMARFSKA
PGNRNMATFG MMDELRHGQL QLFFPHEYCK KDRQFDWAWR AYHSNEWAAI AAKHFFDDII
TGRDAISVAI MLTFSFETGF TNMQFLGLAA DAAEAGDYTF ANLISSIQTD ESRHAQQGGP
ALQLLIENGK REEAQKKVDM AIWRAWRLFA VLTGPVMDYY TPLEDRSQSF KEFMYEWIIG
QFERSLIDLG LDKPWYWDLF LKDIDELHHS YHMGVWYWRT TAWWNPAAGV TPEERDWLEE
KYPGWNKRWG RCWDVITENV LNDRMDLVSP ETLPSVCNMS QIPLVGVPGD DWNIEVFSLE
HNGRLYHFGS EVDRWVFQQD PVQYQNHMNI VDRFLAGQIQ PMTLEGALKY MGFQSIEEMG
KDAHDFAWAD KCKPAMKKSA
