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Quinohemoprotein alcohol dehydrogenase ADH IIB (ADH IIB) (EC 1.1.9.1) (Alcohol dehydrogenase (azurin))

 QHED_PSEPU              Reviewed;         690 AA.
Q8GR64;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
20-JUN-2018, entry version 86.
RecName: Full=Quinohemoprotein alcohol dehydrogenase ADH IIB {ECO:0000303|PubMed:12843671};
Short=ADH IIB {ECO:0000303|PubMed:12843671};
EC=1.1.9.1 {ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
AltName: Full=Alcohol dehydrogenase (azurin) {ECO:0000305};
Flags: Precursor;
Name=qbdA {ECO:0000303|PubMed:12843671};
Pseudomonas putida (Arthrobacter siderocapsulatus).
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=303;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-36; 247-262
AND 388-396, AND MASS SPECTROMETRY.
STRAIN=HK5;
PubMed=12843671; DOI=10.1271/bbb.67.1397;
Toyama H., Fujii T., Aoki N., Matsushita K., Adachi O.;
"Molecular cloning of quinohemoprotein alcohol dehydrogenase, ADH IIB,
from Pseudomonas putida HK5.";
Biosci. Biotechnol. Biochem. 67:1397-1400(2003).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INDUCTION.
STRAIN=HK5;
PubMed=7730276; DOI=10.1128/jb.177.9.2442-2450.1995;
Toyama H., Fujii A., Matsushita K., Shinagawa E., Ameyama M.,
Adachi O.;
"Three distinct quinoprotein alcohol dehydrogenases are expressed when
Pseudomonas putida is grown on different alcohols.";
J. Bacteriol. 177:2442-2450(1995).
[3]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=HK5;
PubMed=10320337; DOI=10.1021/bi990121f;
Matsushita K., Yamashita T., Aoki N., Toyama H., Adachi O.;
"Electron transfer from quinohemoprotein alcohol dehydrogenase to blue
copper protein azurin in the alcohol oxidase respiratory chain of
Pseudomonas putida HK5.";
Biochemistry 38:6111-6118(1999).
[4]
FUNCTION, CATALYTIC ACTIVITY, STEREOSPECIFICITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=HK5;
PubMed=16061256; DOI=10.1016/j.jmb.2005.06.078;
Toyama H., Chen Z.W., Fukumoto M., Adachi O., Matsushita K.,
Mathews F.S.;
"Molecular cloning and structural analysis of quinohemoprotein alcohol
dehydrogenase ADH-IIG from Pseudomonas putida HK5.";
J. Mol. Biol. 352:91-104(2005).
[5]
FUNCTION, AND INDUCTION.
STRAIN=HK5;
PubMed=18218017; DOI=10.1111/j.1574-6968.2008.01060.x;
Promden W., Vangnai A.S., Pongsawasdi P., Adachi O., Matsushita K.,
Toyama H.;
"Disruption of quinoprotein ethanol dehydrogenase gene and adjacent
genes in Pseudomonas putida HK5.";
FEMS Microbiol. Lett. 280:203-209(2008).
[6]
INDUCTION.
STRAIN=HK5;
PubMed=19202108; DOI=10.1099/mic.0.021956-0;
Promden W., Vangnai A.S., Toyama H., Matsushita K., Pongsawasdi P.;
"Analysis of the promoter activities of the genes encoding three
quinoprotein alcohol dehydrogenases in Pseudomonas putida HK5.";
Microbiology 155:594-603(2009).
[7]
CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS),
COFACTOR, AND SUBUNIT.
STRAIN=HK5;
PubMed=10531500; DOI=10.1107/S0907444999010744;
Chen Z., Baruch P., Mathews F.S., Matsushita K., Yamashita T.,
Toyama H., Adachi O.;
"Crystallization and preliminary diffraction studies of two
quinoprotein alcohol dehydrogenases (ADHs): a soluble monomeric ADH
from Pseudomonas putida HK5 (ADH-IIB) and a heterotrimeric membrane-
bound ADH from Gluconobacter suboxydans (ADH-GS).";
Acta Crystallogr. D 55:1933-1936(1999).
[8]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 23-690 IN COMPLEX WITH
CALCIUM ION; HEME C AND PYRROLOQUINOLINE QUINONE, PROTEIN SEQUENCE OF
23-36, COFACTOR, ACTIVE SITE, DISULFIDE BOND, AND SUBUNIT.
STRAIN=HK5;
PubMed=12057198; DOI=10.1016/S0969-2126(02)00774-8;
Chen Z.W., Matsushita K., Yamashita T., Fujii T.A., Toyama H.,
Adachi O., Bellamy H.D., Mathews F.S.;
"Structure at 1.9 A resolution of a quinohemoprotein alcohol
dehydrogenase from Pseudomonas putida HK5.";
Structure 10:837-849(2002).
-!- FUNCTION: Catalyzes the dye-linked oxidation of primary alcohols
to the corresponding aldehydes and the (subsequent) oxidation of
the aldehydes to carboxylic acids. Exhibits activity with longer
mono-alcohols (C-4 to C-7) but not with methanol or glycerol.
Reacts with 1,2-propanediol and 1,3-propanediol but not with sugar
alcohols such as D-sorbitol. {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:18218017,
ECO:0000269|PubMed:7730276}.
-!- CATALYTIC ACTIVITY: A primary alcohol + azurin = an aldehyde +
reduced azurin. {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276}.
-!- COFACTOR:
Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
Evidence={ECO:0000269|PubMed:10531500,
ECO:0000269|PubMed:12057198, ECO:0000269|PubMed:7730276};
Note=Binds 1 PQQ group per subunit. PQQ is inserted between
disulfide Cys-127-Cys-128 and the plane of Trp-254.
{ECO:0000269|PubMed:10531500, ECO:0000269|PubMed:12057198,
ECO:0000269|PubMed:7730276};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:10531500,
ECO:0000269|PubMed:12057198};
Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:10531500,
ECO:0000269|PubMed:12057198};
-!- COFACTOR:
Name=heme c; Xref=ChEBI:CHEBI:61717;
Evidence={ECO:0000269|PubMed:10531500,
ECO:0000269|PubMed:12057198, ECO:0000269|PubMed:7730276};
Note=Binds 1 heme c group per subunit.
{ECO:0000269|PubMed:10531500, ECO:0000269|PubMed:12057198,
ECO:0000269|PubMed:7730276};
-!- ENZYME REGULATION: Inhibited by 10 mM 1-butanol.
{ECO:0000269|PubMed:7730276}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.61 mM for ethanol {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=0.105 mM for butane-1-ol {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=10.2 mM for propane-1,2-diol {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=3.71 mM for (S+)propane-1,2-diol
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
KM=4.58 mM for (R-)propane-1,2-diol
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
KM=0.015 mM for butane-1-ol {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=100 uM for azurin (from P.putida in the presence of 30 mM
Tris-HCl pH 8.0) {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=51 uM for azurin (from P.putida in the presence of 30 mM
Tris-HCl pH 8.0 and 0.1 M KCl) {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=25 uM for azurin (from P.putida in the presence of 30 mM
Tris-HCl pH 8.0 and 0.5 M KCl) {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=202 uM for azurin (from P.aerugionosa in the presence of 30
mM Tris-HCl pH 8.0) {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
KM=95 uM for potassium ferricyanide (in the presence of 30 mM
Tris-HCl pH 8.0 and 0.1 M KCl) {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
Vmax=15.4 umol/min/mg enzyme with ethanol as substrate
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
Vmax=17.1 umol/min/mg enzyme with butane-1-ol as substrate
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
Vmax=4.27 umol/min/mg enzyme with propane-1,2-diol as substrate
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
Vmax=2.61 umol/min/mg enzyme with (S+)propane-1,2-diol as
substrate {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
Vmax=7.10 umol/min/mg enzyme with (R-)propane-1,2-diol as
substrate {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
Vmax=31 umol/min/mg enzyme with butane-1-ol as substrate
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
Vmax=62.5 umol/min/mg enzyme toward azurin (from P.putida in the
presence of 30 mM Tris-HCl pH 8.0) {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
Vmax=52.6 umol/min/mg enzyme toward azurin (from P.putida in the
presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
Vmax=41.7 umol/min/mg enzyme toward azurin (from P.putida in the
presence of 30 mM Tris-HCl pH 8.0 and 0.1 M KCl)
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
Vmax=22.3 umol/min/mg enzyme toward azurin (from P.aeruginosa in
the presence of 30 mM Tris-HCl pH 8.0)
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
Vmax=45.5 umol/min/mg enzyme toward potassium ferricyanide (in
the presence of 30 mM Tris-HCl pH 8.0)
{ECO:0000269|PubMed:10320337, ECO:0000269|PubMed:16061256,
ECO:0000269|PubMed:7730276};
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
Redox potential:
E(0) is +185 mV for heme c at pH 7.0, +188 mV for heme c at pH
8.0, +172 mV for heme c at pH 8.0 and 0.3 M KCl and +189 mV for
ADH IIB-Azurin complex. {ECO:0000269|PubMed:10320337,
ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10531500,
ECO:0000269|PubMed:12057198, ECO:0000269|PubMed:7730276}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- INDUCTION: By 1-butanol. Primary and secondary C3,C4 alcohols as
well as butyraldehyde. {ECO:0000269|PubMed:18218017,
ECO:0000269|PubMed:19202108, ECO:0000269|PubMed:7730276}.
-!- MASS SPECTROMETRY: Mass=73262; Method=MALDI; Range=23-690;
Note=The measured mass is that of QbdA with a single heme bound.;
Evidence={ECO:0000269|PubMed:12843671};
-!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
{ECO:0000305}.
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EMBL; AB091400; BAC15559.1; -; Genomic_DNA.
RefSeq; WP_058541185.1; NZ_LKGZ01000023.1.
PDB; 1KV9; X-ray; 1.90 A; A=23-690.
PDBsum; 1KV9; -.
ProteinModelPortal; Q8GR64; -.
SMR; Q8GR64; -.
DrugBank; DB03205; Pyrroloquinoline Quinone.
PRIDE; Q8GR64; -.
KEGG; ag:BAC15559; -.
KO; K17760; -.
BRENDA; 1.1.9.1; 5092.
BRENDA; 1.2.99.3; 5092.
SABIO-RK; Q8GR64; -.
EvolutionaryTrace; Q8GR64; -.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0070968; F:pyrroloquinoline quinone binding; IDA:UniProtKB.
Gene3D; 1.10.760.10; -; 1.
InterPro; IPR009056; Cyt_c-like_dom.
InterPro; IPR036909; Cyt_c-like_dom_sf.
InterPro; IPR018391; PQQ_beta_propeller_repeat.
InterPro; IPR017512; PQQ_MeOH/EtOH_DH.
InterPro; IPR002372; PQQ_repeat.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR001479; Quinoprotein_DH_CS.
Pfam; PF13442; Cytochrome_CBB3; 1.
Pfam; PF13360; PQQ_2; 2.
SMART; SM00564; PQQ; 5.
SUPFAM; SSF46626; SSF46626; 1.
SUPFAM; SSF50998; SSF50998; 1.
TIGRFAMs; TIGR03075; PQQ_enz_alc_DH; 1.
PROSITE; PS00364; BACTERIAL_PQQ_2; 1.
PROSITE; PS51007; CYTC; 1.
1: Evidence at protein level;
3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
Heme; Iron; Metal-binding; Oxidoreductase; Periplasm; PQQ; Signal.
SIGNAL 1 22 {ECO:0000269|PubMed:12057198,
ECO:0000269|PubMed:12843671}.
CHAIN 23 690 Quinohemoprotein alcohol dehydrogenase
ADH IIB. {ECO:0000269|PubMed:7730276}.
/FTId=PRO_0000419525.
DOMAIN 600 678 Cytochrome c. {ECO:0000255|PROSITE-
ProRule:PRU00433}.
REGION 193 194 Pyrroloquinoline quinone binding.
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
REGION 404 405 Pyrroloquinoline quinone binding.
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
ACT_SITE 317 317 Proton acceptor.
{ECO:0000305|PubMed:12057198}.
METAL 195 195 Calcium. {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
METAL 272 272 Calcium. {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
METAL 317 317 Calcium. {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
METAL 617 617 Iron (heme axial ligand); via tele
nitrogen. {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
METAL 655 655 Iron (heme axial ligand).
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 81 81 Pyrroloquinoline quinone.
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 133 133 Pyrroloquinoline quinone.
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 177 177 Pyrroloquinoline quinone.
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 252 252 Pyrroloquinoline quinone.
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 344 344 Pyrroloquinoline quinone.
{ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 547 547 Pyrroloquinoline quinone; via amide
nitrogen. {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 613 613 Heme c (covalent). {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
BINDING 616 616 Heme c (covalent). {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
DISULFID 127 128 {ECO:0000244|PDB:1KV9,
ECO:0000269|PubMed:12057198}.
HELIX 27 32 {ECO:0000244|PDB:1KV9}.
TURN 33 35 {ECO:0000244|PDB:1KV9}.
TURN 60 62 {ECO:0000244|PDB:1KV9}.
HELIX 63 65 {ECO:0000244|PDB:1KV9}.
STRAND 66 73 {ECO:0000244|PDB:1KV9}.
STRAND 85 87 {ECO:0000244|PDB:1KV9}.
STRAND 90 95 {ECO:0000244|PDB:1KV9}.
HELIX 96 98 {ECO:0000244|PDB:1KV9}.
STRAND 99 104 {ECO:0000244|PDB:1KV9}.
TURN 105 107 {ECO:0000244|PDB:1KV9}.
STRAND 110 114 {ECO:0000244|PDB:1KV9}.
HELIX 120 125 {ECO:0000244|PDB:1KV9}.
STRAND 136 139 {ECO:0000244|PDB:1KV9}.
STRAND 141 145 {ECO:0000244|PDB:1KV9}.
STRAND 149 155 {ECO:0000244|PDB:1KV9}.
TURN 156 158 {ECO:0000244|PDB:1KV9}.
STRAND 161 166 {ECO:0000244|PDB:1KV9}.
STRAND 181 183 {ECO:0000244|PDB:1KV9}.
STRAND 186 189 {ECO:0000244|PDB:1KV9}.
TURN 194 196 {ECO:0000244|PDB:1KV9}.
STRAND 201 206 {ECO:0000244|PDB:1KV9}.
TURN 207 209 {ECO:0000244|PDB:1KV9}.
STRAND 212 219 {ECO:0000244|PDB:1KV9}.
HELIX 230 236 {ECO:0000244|PDB:1KV9}.
HELIX 244 247 {ECO:0000244|PDB:1KV9}.
STRAND 257 260 {ECO:0000244|PDB:1KV9}.
TURN 261 264 {ECO:0000244|PDB:1KV9}.
STRAND 265 269 {ECO:0000244|PDB:1KV9}.
STRAND 273 276 {ECO:0000244|PDB:1KV9}.
HELIX 278 281 {ECO:0000244|PDB:1KV9}.
TURN 289 292 {ECO:0000244|PDB:1KV9}.
STRAND 293 297 {ECO:0000244|PDB:1KV9}.
TURN 299 301 {ECO:0000244|PDB:1KV9}.
STRAND 304 311 {ECO:0000244|PDB:1KV9}.
STRAND 324 331 {ECO:0000244|PDB:1KV9}.
STRAND 334 341 {ECO:0000244|PDB:1KV9}.
STRAND 346 352 {ECO:0000244|PDB:1KV9}.
TURN 353 355 {ECO:0000244|PDB:1KV9}.
STRAND 358 365 {ECO:0000244|PDB:1KV9}.
STRAND 369 373 {ECO:0000244|PDB:1KV9}.
TURN 375 377 {ECO:0000244|PDB:1KV9}.
STRAND 380 382 {ECO:0000244|PDB:1KV9}.
TURN 384 387 {ECO:0000244|PDB:1KV9}.
STRAND 389 391 {ECO:0000244|PDB:1KV9}.
STRAND 393 397 {ECO:0000244|PDB:1KV9}.
STRAND 409 411 {ECO:0000244|PDB:1KV9}.
TURN 412 415 {ECO:0000244|PDB:1KV9}.
STRAND 416 423 {ECO:0000244|PDB:1KV9}.
STRAND 426 428 {ECO:0000244|PDB:1KV9}.
HELIX 432 434 {ECO:0000244|PDB:1KV9}.
HELIX 447 449 {ECO:0000244|PDB:1KV9}.
HELIX 455 457 {ECO:0000244|PDB:1KV9}.
STRAND 459 466 {ECO:0000244|PDB:1KV9}.
TURN 467 470 {ECO:0000244|PDB:1KV9}.
STRAND 471 481 {ECO:0000244|PDB:1KV9}.
STRAND 486 489 {ECO:0000244|PDB:1KV9}.
TURN 490 492 {ECO:0000244|PDB:1KV9}.
STRAND 493 497 {ECO:0000244|PDB:1KV9}.
STRAND 501 507 {ECO:0000244|PDB:1KV9}.
TURN 508 510 {ECO:0000244|PDB:1KV9}.
STRAND 513 518 {ECO:0000244|PDB:1KV9}.
STRAND 528 532 {ECO:0000244|PDB:1KV9}.
STRAND 535 542 {ECO:0000244|PDB:1KV9}.
HELIX 547 551 {ECO:0000244|PDB:1KV9}.
HELIX 554 557 {ECO:0000244|PDB:1KV9}.
STRAND 566 572 {ECO:0000244|PDB:1KV9}.
HELIX 599 612 {ECO:0000244|PDB:1KV9}.
HELIX 614 617 {ECO:0000244|PDB:1KV9}.
HELIX 619 621 {ECO:0000244|PDB:1KV9}.
STRAND 625 627 {ECO:0000244|PDB:1KV9}.
HELIX 630 632 {ECO:0000244|PDB:1KV9}.
HELIX 635 639 {ECO:0000244|PDB:1KV9}.
HELIX 641 647 {ECO:0000244|PDB:1KV9}.
HELIX 651 653 {ECO:0000244|PDB:1KV9}.
TURN 659 661 {ECO:0000244|PDB:1KV9}.
HELIX 664 684 {ECO:0000244|PDB:1KV9}.
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


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