QHED_PSEPU
ID QHED_PSEPU Reviewed; 690 AA.
AC Q8GR64;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Quinohemoprotein alcohol dehydrogenase ADH IIB {ECO:0000303|PubMed:12843671};
DE Short=ADH IIB {ECO:0000303|PubMed:12843671};
DE EC=1.1.9.1 {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
DE AltName: Full=Alcohol dehydrogenase (azurin) {ECO:0000305};
DE Flags: Precursor;
GN Name=qbdA {ECO:0000303|PubMed:12843671};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-36; 247-262 AND
RP 388-396, AND MASS SPECTROMETRY.
RC STRAIN=HK5;
RX PubMed=12843671; DOI=10.1271/bbb.67.1397;
RA Toyama H., Fujii T., Aoki N., Matsushita K., Adachi O.;
RT "Molecular cloning of quinohemoprotein alcohol dehydrogenase, ADH IIB, from
RT Pseudomonas putida HK5.";
RL Biosci. Biotechnol. Biochem. 67:1397-1400(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=HK5;
RX PubMed=7730276; DOI=10.1128/jb.177.9.2442-2450.1995;
RA Toyama H., Fujii A., Matsushita K., Shinagawa E., Ameyama M., Adachi O.;
RT "Three distinct quinoprotein alcohol dehydrogenases are expressed when
RT Pseudomonas putida is grown on different alcohols.";
RL J. Bacteriol. 177:2442-2450(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=HK5;
RX PubMed=10320337; DOI=10.1021/bi990121f;
RA Matsushita K., Yamashita T., Aoki N., Toyama H., Adachi O.;
RT "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue
RT copper protein azurin in the alcohol oxidase respiratory chain of
RT Pseudomonas putida HK5.";
RL Biochemistry 38:6111-6118(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, STEREOSPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=HK5;
RX PubMed=16061256; DOI=10.1016/j.jmb.2005.06.078;
RA Toyama H., Chen Z.W., Fukumoto M., Adachi O., Matsushita K., Mathews F.S.;
RT "Molecular cloning and structural analysis of quinohemoprotein alcohol
RT dehydrogenase ADH-IIG from Pseudomonas putida HK5.";
RL J. Mol. Biol. 352:91-104(2005).
RN [5]
RP FUNCTION, AND INDUCTION.
RC STRAIN=HK5;
RX PubMed=18218017; DOI=10.1111/j.1574-6968.2008.01060.x;
RA Promden W., Vangnai A.S., Pongsawasdi P., Adachi O., Matsushita K.,
RA Toyama H.;
RT "Disruption of quinoprotein ethanol dehydrogenase gene and adjacent genes
RT in Pseudomonas putida HK5.";
RL FEMS Microbiol. Lett. 280:203-209(2008).
RN [6]
RP INDUCTION.
RC STRAIN=HK5;
RX PubMed=19202108; DOI=10.1099/mic.0.021956-0;
RA Promden W., Vangnai A.S., Toyama H., Matsushita K., Pongsawasdi P.;
RT "Analysis of the promoter activities of the genes encoding three
RT quinoprotein alcohol dehydrogenases in Pseudomonas putida HK5.";
RL Microbiology 155:594-603(2009).
RN [7]
RP CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS),
RP COFACTOR, AND SUBUNIT.
RC STRAIN=HK5;
RX PubMed=10531500; DOI=10.1107/s0907444999010744;
RA Chen Z., Baruch P., Mathews F.S., Matsushita K., Yamashita T., Toyama H.,
RA Adachi O.;
RT "Crystallization and preliminary diffraction studies of two quinoprotein
RT alcohol dehydrogenases (ADHs): a soluble monomeric ADH from Pseudomonas
RT putida HK5 (ADH-IIB) and a heterotrimeric membrane-bound ADH from
RT Gluconobacter suboxydans (ADH-GS).";
RL Acta Crystallogr. D 55:1933-1936(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 23-690 IN COMPLEX WITH CALCIUM
RP ION; HEME C AND PYRROLOQUINOLINE QUINONE, PROTEIN SEQUENCE OF 23-36,
RP COFACTOR, ACTIVE SITE, DISULFIDE BOND, AND SUBUNIT.
RC STRAIN=HK5;
RX PubMed=12057198; DOI=10.1016/s0969-2126(02)00774-8;
RA Chen Z.W., Matsushita K., Yamashita T., Fujii T.A., Toyama H., Adachi O.,
RA Bellamy H.D., Mathews F.S.;
RT "Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase
RT from Pseudomonas putida HK5.";
RL Structure 10:837-849(2002).
CC -!- FUNCTION: Catalyzes the dye-linked oxidation of primary alcohols to the
CC corresponding aldehydes and the (subsequent) oxidation of the aldehydes
CC to carboxylic acids. Exhibits activity with longer mono-alcohols (C-4
CC to C-7) but not with methanol or glycerol. Reacts with 1,2-propanediol
CC and 1,3-propanediol but not with sugar alcohols such as D-sorbitol.
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:18218017, ECO:0000269|PubMed:7730276}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + 2 oxidized [azurin] = an aldehyde + 2 H(+)
CC + 2 reduced [azurin]; Xref=Rhea:RHEA:51148, Rhea:RHEA-COMP:11034,
CC Rhea:RHEA-COMP:11035, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552; EC=1.1.9.1;
CC Evidence={ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:10531500, ECO:0000269|PubMed:12057198,
CC ECO:0000269|PubMed:7730276};
CC Note=Binds 1 PQQ group per subunit. PQQ is inserted between disulfide
CC Cys-127-Cys-128 and the plane of Trp-254. {ECO:0000269|PubMed:10531500,
CC ECO:0000269|PubMed:12057198, ECO:0000269|PubMed:7730276};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10531500, ECO:0000269|PubMed:12057198};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10531500,
CC ECO:0000269|PubMed:12057198};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:10531500, ECO:0000269|PubMed:12057198,
CC ECO:0000269|PubMed:7730276};
CC Note=Binds 1 heme c group per subunit. {ECO:0000269|PubMed:10531500,
CC ECO:0000269|PubMed:12057198, ECO:0000269|PubMed:7730276};
CC -!- ACTIVITY REGULATION: Inhibited by 10 mM 1-butanol.
CC {ECO:0000269|PubMed:7730276}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.61 mM for ethanol {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=0.105 mM for butane-1-ol {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=10.2 mM for propane-1,2-diol {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=3.71 mM for (S+)propane-1,2-diol {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=4.58 mM for (R-)propane-1,2-diol {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=0.015 mM for butane-1-ol {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=100 uM for azurin (from P.putida in the presence of 30 mM Tris-HCl
CC pH 8.0) {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC KM=51 uM for azurin (from P.putida in the presence of 30 mM Tris-HCl
CC pH 8.0 and 0.1 M KCl) {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=25 uM for azurin (from P.putida in the presence of 30 mM Tris-HCl
CC pH 8.0 and 0.5 M KCl) {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=202 uM for azurin (from P.aerugionosa in the presence of 30 mM
CC Tris-HCl pH 8.0) {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC KM=95 uM for potassium ferricyanide (in the presence of 30 mM Tris-
CC HCl pH 8.0 and 0.1 M KCl) {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=15.4 umol/min/mg enzyme with ethanol as substrate
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=17.1 umol/min/mg enzyme with butane-1-ol as substrate
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=4.27 umol/min/mg enzyme with propane-1,2-diol as substrate
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=2.61 umol/min/mg enzyme with (S+)propane-1,2-diol as substrate
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=7.10 umol/min/mg enzyme with (R-)propane-1,2-diol as substrate
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=31 umol/min/mg enzyme with butane-1-ol as substrate
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=62.5 umol/min/mg enzyme toward azurin (from P.putida in the
CC presence of 30 mM Tris-HCl pH 8.0) {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=52.6 umol/min/mg enzyme toward azurin (from P.putida in the
CC presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=41.7 umol/min/mg enzyme toward azurin (from P.putida in the
CC presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)
CC {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=22.3 umol/min/mg enzyme toward azurin (from P.aeruginosa in the
CC presence of 30 mM Tris-HCl pH 8.0) {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=45.5 umol/min/mg enzyme toward potassium ferricyanide (in the
CC presence of 30 mM Tris-HCl pH 8.0) {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Redox potential:
CC E(0) is +185 mV for heme c at pH 7.0, +188 mV for heme c at pH 8.0,
CC +172 mV for heme c at pH 8.0 and 0.3 M KCl and +189 mV for ADH IIB-
CC Azurin complex. {ECO:0000269|PubMed:10320337,
CC ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10531500,
CC ECO:0000269|PubMed:12057198, ECO:0000269|PubMed:7730276}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- INDUCTION: By 1-butanol. Primary and secondary C3,C4 alcohols as well
CC as butyraldehyde. {ECO:0000269|PubMed:18218017,
CC ECO:0000269|PubMed:19202108, ECO:0000269|PubMed:7730276}.
CC -!- MASS SPECTROMETRY: Mass=73262; Method=MALDI; Note=The measured mass is
CC that of QbdA with a single heme bound.;
CC Evidence={ECO:0000269|PubMed:12843671};
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB091400; BAC15559.1; -; Genomic_DNA.
DR RefSeq; WP_058541185.1; NZ_LKGZ01000023.1.
DR PDB; 1KV9; X-ray; 1.90 A; A=23-690.
DR PDBsum; 1KV9; -.
DR AlphaFoldDB; Q8GR64; -.
DR SMR; Q8GR64; -.
DR DrugBank; DB03205; Pyrroloquinoline Quinone.
DR KEGG; ag:BAC15559; -.
DR BRENDA; 1.1.9.1; 5092.
DR BRENDA; 1.2.5.2; 5092.
DR SABIO-RK; Q8GR64; -.
DR EvolutionaryTrace; Q8GR64; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR GO; GO:0070968; F:pyrroloquinoline quinone binding; IDA:UniProtKB.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
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; PF13442; Cytochrome_CBB3; 1.
DR Pfam; PF13360; PQQ_2; 2.
DR SMART; SM00564; PQQ; 5.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
DR PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; Heme;
KW Iron; Metal-binding; Oxidoreductase; Periplasm; PQQ; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0000269|PubMed:12843671"
FT CHAIN 23..690
FT /note="Quinohemoprotein alcohol dehydrogenase ADH IIB"
FT /evidence="ECO:0000269|PubMed:7730276"
FT /id="PRO_0000419525"
FT DOMAIN 600..678
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 317
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:12057198"
FT BINDING 81
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 133
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 177
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 193..194
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 252
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 344
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 404..405
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 547
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 613
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 616
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 617
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT BINDING 655
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT DISULFID 127..128
FT /evidence="ECO:0000269|PubMed:12057198,
FT ECO:0007744|PDB:1KV9"
FT HELIX 27..32
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 304..311
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 324..331
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 412..415
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 416..423
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 471..481
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 508..510
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 535..542
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 547..551
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 599..612
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 619..621
FT /evidence="ECO:0007829|PDB:1KV9"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 630..632
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 635..639
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 641..647
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:1KV9"
FT TURN 659..661
FT /evidence="ECO:0007829|PDB:1KV9"
FT HELIX 664..684
FT /evidence="ECO:0007829|PDB:1KV9"
SQ SEQUENCE 690 AA; 74969 MW; F5198701D0937613 CRC64;
MKKPLRTSLL MLCLATPLAA LAAGVDEAAI RATEQAGGEW LSHGRTYAEQ RFSPLKQIDA
SNVRSLGLAW YMDLDNTRGL EATPLFHDGV IYTSMSWSRV IAVDAASGKE LWRYDPEVAK
VKARTSCCDA VNRGVALWGD KVYVGTLDGR LIALDAKTGK AIWSQQTTDP AKPYSITGAP
RVVKGKVIIG NGGAEYGVRG FVSAYDADTG KLAWRFYTVP GDPALPYEHP ELREAAKTWQ
GDQYWKLGGG GTVWDSMAYD PELDLLYVGT GNGSPWNREV RSPGGGDNLY LSSILAIRPD
TGKLAWHYQV TPGDSWDFTA TQQITLAELN IDGKPRKVLM QAPKNGFFYV LDRTNGKLIS
AEKFGKVTWA EKVDLATGRP VEAPGVRYEK EPIVMWPSPF GAHNWHSMSF NPGTGLVYIP
YQEVPGVYRN EGKDFVTRKA FNTAAGFADA TDVPAAVVSG ALLAWDPVKQ KAAWKVPYPT
HWNGGTLSTA GNLVFQGTAA GQMHAYSADK GEALWQFEAQ SGIVAAPMTF ELAGRQYVAI
MAGWGGVATL TGGESMNLPG MKNRSRLLVF ALDGKAQLPP PAPAPAKVER VPQPVTAAPE
QVQAGKQLYG QFCSVCHGMG TISGGLIPDL RQSSDATREH FQQIVLQGAL KPLGMPSFDD
SLKPEEVEQI KLYVMSREYE DYMARHKAAP
