QEDH_PSEAE
ID QEDH_PSEAE Reviewed; 623 AA.
AC Q9Z4J7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Quinoprotein ethanol dehydrogenase {ECO:0000303|PubMed:19224199, ECO:0000303|PubMed:3144289, ECO:0000303|PubMed:9826187};
DE Short=QEDH {ECO:0000303|PubMed:19224199, ECO:0000303|PubMed:9826187};
DE EC=1.1.2.8 {ECO:0000269|PubMed:19224199, ECO:0000269|PubMed:8380982, ECO:0000305|PubMed:3144289};
DE AltName: Full=Quinoprotein alcohol dehydrogenase (cytochrome c) {ECO:0000305};
DE AltName: Full=Quinoprotein alcohol dehydrogenase (cytochrome c550) {ECO:0000305};
DE Flags: Precursor;
GN Name=exaA {ECO:0000303|PubMed:10075429}; OrderedLocusNames=PA1982;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 35-46, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC STRAIN=ATCC 17933;
RX PubMed=9826187; DOI=10.1046/j.1432-1327.1998.2570409.x;
RA Diehl A., von Wintzingerode F., Gorisch H.;
RT "Quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa is a
RT homodimer: sequence of the gene and deduced structural properties of the
RT enzyme.";
RL Eur. J. Biochem. 257:409-419(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52, AND PATHWAY.
RC STRAIN=ATCC 17933;
RX PubMed=10075429; DOI=10.1099/13500872-145-2-471;
RA Schobert M., Goerisch H.;
RT "Cytochrome c550 is an essential component of the quinoprotein ethanol
RT oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the
RT genes encoding cytochrome c550 and an adjacent acetaldehyde
RT dehydrogenase.";
RL Microbiology 145:471-481(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP ACTIVITY REGULATION, SUBUNIT, SUBSTRATE SPECIFICITY, AND INDUCTION.
RC STRAIN=ATCC 17933;
RX PubMed=3144289; DOI=10.1515/bchm3.1988.369.1.431;
RA Rupp M., Goerisch H.;
RT "Purification, crystallisation and characterization of quinoprotein ethanol
RT dehydrogenase from Pseudomonas aeruginosa.";
RL Biol. Chem. Hoppe-Seyler 369:431-439(1988).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 17933;
RX PubMed=8380982; DOI=10.1042/bj2890173;
RA Reichmann P., Goerisch H.;
RT "Cytochrome c550 from Pseudomonas aeruginosa.";
RL Biochem. J. 289:173-178(1993).
RN [6]
RP COFACTOR, AND MUTAGENESIS OF 139-CYS-CYS-140.
RC STRAIN=ATCC 17933;
RX PubMed=15094044; DOI=10.1016/s0014-5793(04)00317-5;
RA Kay C.W., Mennenga B., Goerisch H., Bittl R.;
RT "Characterisation of the PQQ cofactor radical in quinoprotein ethanol
RT dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance
RT spectroscopy.";
RL FEBS Lett. 564:69-72(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP MUTAGENESIS OF 139-CYS-CYS-140, AND INTERACTION WITH CYTOCHROME C550.
RC STRAIN=ATCC 17933;
RX PubMed=19224199; DOI=10.1007/s00203-009-0460-4;
RA Mennenga B., Kay C.W., Goerisch H.;
RT "Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the
RT unusual disulfide ring formed by adjacent cysteine residues is essential
RT for efficient electron transfer to cytochrome c550.";
RL Arch. Microbiol. 191:361-367(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 35-616 IN COMPLEX WITH CALCIUM
RP IONS AND PYRROLOQUINOLINE QUINONE, COFACTOR, SUBUNIT, AND DISULFIDE BOND.
RC STRAIN=ATCC 17933;
RX PubMed=10736230; DOI=10.1006/jmbi.2000.3603;
RA Keitel T., Diehl A., Knaute T., Stezowski J.J., Hoehne W., Goerisch H.;
RT "X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas
RT aeruginosa: basis of substrate specificity.";
RL J. Mol. Biol. 297:961-974(2000).
CC -!- FUNCTION: Catalyzes the oxidation of ethanol and other primary alcohols
CC to the corresponding aldehydes, except methanol, which is a very poor
CC substrate. Uses a specific inducible cytochrome c550, encoded by the
CC adjacent gene in the locus, as electron acceptor. Is a key enzyme of
CC the carbon and energy metabolism during growth of P.aeruginosa on
CC ethanol as the sole carbon and energy source. Is also able to use
CC secondary alcohols as well as aminoalcohols like ethanolamine and 1-
CC amino-2-propanol, and aldehydes as substrates.
CC {ECO:0000269|PubMed:19224199, ECO:0000269|PubMed:3144289,
CC ECO:0000269|PubMed:8380982}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + 2 Fe(III)-[cytochrome c] = an aldehyde + 2
CC Fe(II)-[cytochrome c] + 2 H(+); Xref=Rhea:RHEA:51020, Rhea:RHEA-
CC COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=1.1.2.8; Evidence={ECO:0000269|PubMed:19224199,
CC ECO:0000269|PubMed:8380982, ECO:0000305|PubMed:3144289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51021;
CC Evidence={ECO:0000305|PubMed:8380982};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + 2 Fe(III)-[cytochrome c] = acetaldehyde + 2 Fe(II)-
CC [cytochrome c] + 2 H(+); Xref=Rhea:RHEA:62200, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:8380982, ECO:0000305|PubMed:19224199,
CC ECO:0000305|PubMed:3144289};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62201;
CC Evidence={ECO:0000305|PubMed:8380982};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butan-1-ol + 2 Fe(III)-[cytochrome c] = butanal + 2 Fe(II)-
CC [cytochrome c] + 2 H(+); Xref=Rhea:RHEA:43432, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15743,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000305|PubMed:19224199, ECO:0000305|PubMed:3144289};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + propan-2-ol = acetone + 2 Fe(II)-
CC [cytochrome c] + 2 H(+); Xref=Rhea:RHEA:62196, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15347, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17824, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000269|PubMed:19224199};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-propanol + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome
CC c] + 2 H(+) + propanal; Xref=Rhea:RHEA:62204, Rhea:RHEA-COMP:10350,
CC Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153,
CC ChEBI:CHEBI:28831, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034;
CC Evidence={ECO:0000305|PubMed:19224199};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:10736230, ECO:0000269|PubMed:15094044,
CC ECO:0000269|PubMed:19224199, ECO:0000269|PubMed:3144289};
CC Note=Binds 1 PQQ group non-covalently per subunit (PubMed:10736230,
CC PubMed:3144289). PQQ is embedded between the ring structure formed from
CC a disulfide bridge between adjacent cysteines Cys-139 and Cys-140 and
CC the indole ring of Trp-282 (PubMed:10736230).
CC {ECO:0000269|PubMed:10736230, ECO:0000269|PubMed:3144289};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10736230, ECO:0000269|PubMed:19224199,
CC ECO:0000305|PubMed:3144289};
CC Note=Binds 2 calcium ions per subunit. One is located in the active-
CC site cavity near PQQ and the second calcium binds at the N-terminus and
CC contributes to the stability of the native enzyme.
CC {ECO:0000269|PubMed:10736230};
CC -!- ACTIVITY REGULATION: Inhibited by cyclopropanone ethylhemiketal.
CC Activated by ammonia (500mM), methylamine (5mM), ethylamine (5mM),
CC octylamine (5mM), ethanolamine (5mM) and 1-amino-2-propanol (5mM), in
CC assays using artificial electron acceptors (PubMed:3144289). Ammonia is
CC not needed for, nor does it stimulate, the ethanol-oxidizing activity
CC when using the natural electron acceptor cytochrome c550
CC (PubMed:8380982). {ECO:0000269|PubMed:3144289,
CC ECO:0000269|PubMed:8380982}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for ethanol {ECO:0000269|PubMed:3144289};
CC KM=21 uM for 1-propanol {ECO:0000269|PubMed:3144289};
CC KM=680 uM for 2-propanol {ECO:0000269|PubMed:3144289};
CC KM=980 uM for (2S)-2-butanol {ECO:0000269|PubMed:3144289};
CC KM=4.5 mM for ethanal {ECO:0000269|PubMed:3144289};
CC KM=94 mM for methanol {ECO:0000269|PubMed:3144289};
CC KM=12 uM for ethanol (at pH 9) {ECO:0000269|PubMed:19224199};
CC KM=62 uM for 1-propanol (at pH 9) {ECO:0000269|PubMed:19224199};
CC KM=1.4 mM for 2-propanol (at pH 9) {ECO:0000269|PubMed:19224199};
CC KM=21 mM for 1,3-propanediol (at pH 9) {ECO:0000269|PubMed:19224199};
CC KM=0.43 mM for 1-butanol (at pH 9) {ECO:0000269|PubMed:19224199};
CC Note=kcat is 11 sec(-1) for the oxidation of ethanol using artificial
CC electron acceptor (at pH 9). kcat is 15 sec(-1) for the oxidation of
CC 1-propanol using artificial electron acceptor (at pH 9). kcat is 11
CC sec(-1) for the oxidation of 2-propanol using artificial electron
CC acceptor (at pH 9). kcat is 40 sec(-1) for the oxidation of 1,3-
CC propanediol using artificial electron acceptor (at pH 9). kcat is 42
CC sec(-1) for the oxidation of 1-butanol using artificial electron
CC acceptor (at pH 9). kcat is 2.4 sec(-1) for the oxidation of 2-
CC propanol using natural electron acceptor cytochrome c550 (at pH 7).
CC {ECO:0000269|PubMed:19224199};
CC pH dependence:
CC Optimum pH is 9 in assays using artificial electron acceptors
CC (PubMed:3144289). However, in a system with homogenous QEDH,
CC cytochrome c550 and a membrane fraction of P.aeruginosa, electron
CC transport from ethanol to O(2) is observed at the more physiological
CC conditions of pH 7, and the system is inactive at pH 9
CC (PubMed:8380982). {ECO:0000269|PubMed:3144289,
CC ECO:0000269|PubMed:8380982};
CC -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC step 1/2. {ECO:0000305|PubMed:10075429}.
CC -!- SUBUNIT: Homodimer. Interacts with cytochrome c550 (PubMed:19224199).
CC {ECO:0000269|PubMed:10736230, ECO:0000269|PubMed:19224199,
CC ECO:0000269|PubMed:3144289, ECO:0000269|PubMed:9826187}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:9826187}.
CC -!- INDUCTION: Induced by growth on ethanol. {ECO:0000269|PubMed:3144289}.
CC -!- PTM: The disulfide ring formed between the two adjacent cysteine
CC residues Cys-139 and Cys-140 is essential for efficient electron
CC transfer at pH 7 from QEDH to its natural electron acceptor cytochrome
CC c550. {ECO:0000269|PubMed:19224199}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ009858; CAA08896.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05370.1; -; Genomic_DNA.
DR EMBL; AF068264; AAC79657.1; -; Genomic_DNA.
DR PIR; B83399; B83399.
DR RefSeq; NP_250672.1; NC_002516.2.
DR RefSeq; WP_003088524.1; NZ_QZGE01000030.1.
DR PDB; 1FLG; X-ray; 2.60 A; A/B=35-616.
DR PDBsum; 1FLG; -.
DR AlphaFoldDB; Q9Z4J7; -.
DR SMR; Q9Z4J7; -.
DR STRING; 287.DR97_5865; -.
DR DrugBank; DB03205; Pyrroloquinoline Quinone.
DR PaxDb; Q9Z4J7; -.
DR PRIDE; Q9Z4J7; -.
DR EnsemblBacteria; AAG05370; AAG05370; PA1982.
DR GeneID; 880475; -.
DR KEGG; pae:PA1982; -.
DR PATRIC; fig|208964.12.peg.2066; -.
DR PseudoCAP; PA1982; -.
DR HOGENOM; CLU_018478_0_0_6; -.
DR InParanoid; Q9Z4J7; -.
DR OMA; YVPANEW; -.
DR PhylomeDB; Q9Z4J7; -.
DR BioCyc; MetaCyc:MON-15517; -.
DR BioCyc; PAER208964:G1FZ6-2020-MON; -.
DR BRENDA; 1.1.2.8; 5087.
DR BRENDA; 1.1.2.B3; 5087.
DR UniPathway; UPA00780; UER00767.
DR EvolutionaryTrace; Q9Z4J7; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0052934; F:alcohol dehydrogenase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006069; P:ethanol oxidation; IDA:PseudoCAP.
DR CDD; cd10277; PQQ_ADH_I; 1.
DR InterPro; IPR034119; ADHI.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
DR InterPro; IPR002372; PQQ_repeat.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR001479; Quinoprotein_DH_CS.
DR Pfam; PF01011; PQQ; 1.
DR Pfam; PF13360; PQQ_2; 1.
DR SMART; SM00564; PQQ; 6.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR PROSITE; PS00363; BACTERIAL_PQQ_1; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Oxidoreductase; Periplasm; PQQ; Reference proteome; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:9826187,
FT ECO:0000305|PubMed:3144289"
FT CHAIN 35..623
FT /note="Quinoprotein ethanol dehydrogenase"
FT /id="PRO_0000025565"
FT REGION 244..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 350
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:10736230"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 51
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 95
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 145
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 189
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 207..209
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 378
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 523
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT BINDING 587
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT DISULFID 139..140
FT /evidence="ECO:0000269|PubMed:10736230,
FT ECO:0007744|PDB:1FLG"
FT MUTAGEN 139..140
FT /note="CC->AA: 15-fold decrease in catalytic activity with
FT the natural electron acceptor cytochrome c550. Does not
FT affect, or even increases, catalytic activity with
FT artificial electron acceptors. Shows high decreased
FT affinity for primary alcohols, while the affinity for the
FT secondary alcohol 2-propanol is unaltered."
FT /evidence="ECO:0000269|PubMed:15094044,
FT ECO:0000269|PubMed:19224199"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 392..400
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 512..520
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 541..547
FT /evidence="ECO:0007829|PDB:1FLG"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 575..582
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:1FLG"
FT HELIX 594..599
FT /evidence="ECO:0007829|PDB:1FLG"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:1FLG"
SQ SEQUENCE 623 AA; 68123 MW; 32DDE5DF20B291D6 CRC64;
MTTRTSPAPA GLLRPSLHCL AFAVALGSAG AALAKDVTWE DIANDDKTTG DVLQYGMGTH
AQRWSPLKQV NADNVFKLTP AWSYSFGDEK QRGQESQAIV SDGVIYVTAS YSRLFALDAK
TGKRLWTYNH RLPDDIRPCC DVVNRGAAIY GDKVFFGTLD ASVVALNKNT GKVVWKKKFA
DHGAGYTMTG APTIVKDGKT GKVLLIHGSS GDEFGVVGRL FARDPDTGEE IWMRPFVEGH
MGRLNGKDST VTGDVKAPSW PDDRNSPTGK VESWSHGGGA PWQSASFDAE TNTIIVGAGN
PGPWNTWART AKGGNPHDYD SLYTSGQVGV DPSSGEVKWF YQHTPNDAWD FSGNNELVLF
DYKAKDGKIV KATAHADRNG FFYVVDRSNG KLQNAFPFVD NITWASHIDL KTGRPVEREG
QRPPLPEPGQ KHGKAVEVSP PFLGGKNWNP MAYSQDTGLF YVPANHWKED YWTEEVSYTK
GSAYLGMGFR IKRMYDDHVG SLRAMDPVSG KVVWEHKEHL PLWAGVLATA GNLVFTGTGD
GYFKAFDAKS GKELWKFQTG SGIVSPPITW EQDGEQYLGV TVGYGGAVPL WGGDMADLTR
PVAQGGSFWV FKLPSWDNRT ASR
