QGDA_PSEPU
ID QGDA_PSEPU Reviewed; 718 AA.
AC Q4W6G0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Quinohemoprotein alcohol dehydrogenase ADH-IIG {ECO:0000303|PubMed:16061256};
DE Short=ADH IIG {ECO:0000303|PubMed:7730276};
DE EC=1.1.9.1 {ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
DE AltName: Full=Alcohol dehydrogenase (azurin) {ECO:0000305};
DE Flags: Precursor;
GN Name=qgdA {ECO:0000303|PubMed:16061256};
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 30-40 AND 102-111,
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 30-718 IN COMPLEX WITH SUBSTRATE;
RP CALCIUM ION; HEME C AND PYRROLOQUINOLINE QUINONE, FUNCTION, CATALYTIC
RP ACTIVITY, STEREOSELECTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ACTIVE SITE,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND DISULFIDE
RP BOND.
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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBSTRATE
RP SPECIFICITY, 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, 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 [4]
RP FUNCTION, INDUCTION, AND STEREOSPECIFICITY.
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).
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. Active with primary alcohols, glycerol, 1,2-
CC propanediol, 1,3-propanediol but not with methanol or sugar alcohols
CC such as D-sorbitol. {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:18218017, ECO:0000269|PubMed:19202108,
CC 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:16061256, ECO:0000269|PubMed:7730276};
CC -!- COFACTOR:
CC Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442;
CC Evidence={ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Note=Binds 1 PQQ group per subunit. PQQ is inserted between disulfide
CC Cys-138-Cys-139 and the plane of Trp-266. {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:16061256};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:16061256};
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Note=Binds 1 heme c group per subunit. {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC -!- ACTIVITY REGULATION: Exhibits higher affinity for 1-butanol compared to
CC 1,2-propanediol but inhibited by 10 mM 1-butanol.
CC {ECO:0000269|PubMed:7730276}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=33.2 mM for ethanol {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC KM=0.226 mM for propane-1,2-diol {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC KM=2.40 mM for glycerol {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC KM=0.055 mM for (S+)propane-1,2-diol {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC KM=3.32 mM for (R-)propane-1,2-diol {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC KM=0.043 mM for butane-1-ol {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC Vmax=11.5 umol/min/mg enzyme with ethanol as substrate
CC {ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=17.4 umol/min/mg enzyme with propane-1,2-diol as substrate
CC {ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=17.4 umol/min/mg enzyme with glycerol as substrate
CC {ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=21 umol/min/mg enzyme with (S+)propane-1,2-diol as substrate
CC {ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=12.2 umol/min/mg enzyme with (R-)propane-1,2-diol as substrate
CC {ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC Vmax=8.50 umol/min/mg enzyme with butane-1-ol as substrate
CC {ECO:0000269|PubMed:16061256, ECO:0000269|PubMed:7730276};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16061256,
CC ECO:0000269|PubMed:7730276}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:16061256}.
CC -!- INDUCTION: (S+)-propane-1,2-diol is the most effective whereas (R-)-
CC propane-1,2-diol, ethanediol and glycerol are weaker inducers.
CC {ECO:0000269|PubMed:18218017, ECO:0000269|PubMed:19202108,
CC ECO:0000269|PubMed:7730276}.
CC -!- SIMILARITY: Belongs to the bacterial PQQ dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB204833; BAD99293.1; -; Genomic_DNA.
DR PDB; 1YIQ; X-ray; 2.20 A; A=30-718.
DR PDBsum; 1YIQ; -.
DR AlphaFoldDB; Q4W6G0; -.
DR SMR; Q4W6G0; -.
DR BRENDA; 1.2.5.2; 5092.
DR EvolutionaryTrace; Q4W6G0; -.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0050039; F:lactaldehyde reductase (NADPH) activity; IDA:UniProtKB.
DR GO; GO:0070968; F:pyrroloquinoline quinone binding; IDA:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; 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 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; 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..29
FT /evidence="ECO:0000269|PubMed:16061256"
FT CHAIN 30..718
FT /note="Quinohemoprotein alcohol dehydrogenase ADH-IIG"
FT /evidence="ECO:0000269|PubMed:7730276"
FT /id="PRO_0000419526"
FT DOMAIN 622..699
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT ACT_SITE 329
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16061256"
FT BINDING 92
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 144
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 189
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 205..206
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 264
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 356
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 415
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 419..420
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 571
FT /ligand="pyrroloquinoline quinone"
FT /ligand_id="ChEBI:CHEBI:58442"
FT /evidence="ECO:0000250|UniProtKB:Q46444"
FT BINDING 635
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 638
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 639
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:16061256,
FT ECO:0007744|PDB:1YIQ"
FT BINDING 676
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:16061256,
FT ECO:0007744|PDB:1YIQ"
FT DISULFID 138..139
FT /evidence="ECO:0000269|PubMed:16061256"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 224..231
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 242..248
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 273..276
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 370..377
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 396..399
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 472..479
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 483..490
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 495..505
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 537..542
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 559..566
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 572..575
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 590..596
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 621..634
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 636..639
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 641..643
FT /evidence="ECO:0007829|PDB:1YIQ"
FT STRAND 647..649
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 657..661
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 663..667
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 668..671
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:1YIQ"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 685..704
FT /evidence="ECO:0007829|PDB:1YIQ"
FT HELIX 710..712
FT /evidence="ECO:0007829|PDB:1YIQ"
SQ SEQUENCE 718 AA; 78113 MW; DF407A59574CE7F9 CRC64;
MRQTGLASLP LKSLAVAVLL SLAGTPALAA DIPANVDGAR IIAADKEPGN WMSTGRTYDE
QRYSPLKQIS DQNVGQLGLA WSYKLDLDRG VEATPIVVDG AMYTTGPFSV VYALDARDGR
LIWKYDPQSD RHRAGEACCD AVNRGVAVWK GKVYVGVLDG RLEAIDAKTG QRAWSVDTRA
DHKRSYTITG APRVVNGKVV IGNGGAEFGV RGYVTAYDAE TGKEAWRFYT VPGDPKLPPE
GKGMEIAAKT WFGDAYVEQG GGGTAWDSFA YDPELNLLYI GVGNGSLWDP KWRSQAKGDN
LFLSSIVAVN ADTGEYVWHY QTTPGDAWDY TATQHMILAE LPIDGKPRKV LMQAPKNGFF
YVIDRATGEL LSAKGIVPQS WTKGMDMKTG RPILDEENAA YWKNGKRNLV TPAFWGAHDW
QPMSYNPDTG LVYIPAHIMS AYYEHIPEAP KRNPFKSMYQ LGLRTGMMPE GAEGLLEMAK
SWSGKLIAWD PVKQQAAWEV PYVTIFNGGT LSTAGNLVFE GSADGRVIAY AADTGEKLWE
QPAASGVMAA PVTYSVDGEQ YVTFMAGWGG AFSTFAGALS LRAGVQPYAQ VLTYKLGGTA
KLQEPAPRPD TPKPPALSND TASIEAGAKL YDGYCSQCHG IHAVSGGVLP DLRKLTPEKH
QMFLGILFGG RVPDGMPSFA DAFTPEQVDQ IHQYLIKRAH DLHQEGDTWK QFSAKSSH
