PHHY_PSEAE
ID PHHY_PSEAE Reviewed; 394 AA.
AC P20586;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=p-hydroxybenzoate hydroxylase {ECO:0000303|PubMed:1910043};
DE Short=PHBH {ECO:0000303|PubMed:1910043};
DE EC=1.14.13.2 {ECO:0000269|PubMed:1910043};
DE AltName: Full=4-hydroxybenzoate 3-monooxygenase {ECO:0000305};
GN Name=pobA {ECO:0000303|PubMed:2465205}; OrderedLocusNames=PA0247;
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].
RX PubMed=2465205; DOI=10.1016/0378-1119(88)90044-3;
RA Entsch B., Nan Y., Weaich K., Scott K.F.;
RT "Sequence and organization of pobA, the gene coding for p-hydroxybenzoate
RT hydroxylase, an inducible enzyme from Pseudomonas aeruginosa.";
RL Gene 71:279-291(1988).
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 FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-201 AND TYR-385, AND
RP COFACTOR.
RX PubMed=1910043; DOI=10.1016/s0021-9258(19)47379-1;
RA Entsch B., Palfey B.A., Ballou D.P., Massey V.;
RT "Catalytic function of tyrosine residues in para-hydroxybenzoate
RT hydroxylase as determined by the study of site-directed mutants.";
RL J. Biol. Chem. 266:17341-17349(1991).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS PHE-201; ASP-300 AND
RP PHE-385 IN COMPLEX WITH SUBSTRATE AND FAD, FUNCTION, MUTAGENESIS OF
RP TYR-201; ASN-300 AND TYR-385, COFACTOR, AND SUBUNIT.
RX PubMed=8312276; DOI=10.1021/bi00172a036;
RA Lah M.S., Palfey B.A., Schreuder H.A., Ludwig M.L.;
RT "Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate
RT hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.";
RL Biochemistry 33:1555-1564(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND FAD,
RP FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=7939628; DOI=10.1126/science.7939628;
RA Gatti D.L., Palfey B.A., Lah M.S., Entsch B., Massey V., Ballou D.P.,
RA Ludwig M.L.;
RT "The mobile flavin of 4-OH benzoate hydroxylase.";
RL Science 266:110-114(1994).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND
RP FAD, FUNCTION, COFACTOR, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=8555229; DOI=10.1021/bi951344i;
RA Gatti D.L., Entsch B., Ballou D.P., Ludwig M.L.;
RT "pH-dependent structural changes in the active site of p-hydroxybenzoate
RT hydroxylase point to the importance of proton and water movements during
RT catalysis.";
RL Biochemistry 35:567-578(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND FAD
RP ANALOG, FUNCTION, AND SUBUNIT.
RX PubMed=10600126; DOI=10.1021/bi991603u;
RA Ortiz-Maldonado M., Gatti D., Ballou D.P., Massey V.;
RT "Structure-function correlations of the reaction of reduced nicotinamide
RT analogues with p-hydroxybenzoate hydroxylase substituted with a series of
RT 8-substituted flavins.";
RL Biochemistry 38:16636-16647(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT GLN-220 IN COMPLEX WITH
RP SUBSTRATE AND FAD, FUNCTION, MUTAGENESIS OF ARG-220, COFACTOR, AND SUBUNIT.
RX PubMed=11805318; DOI=10.1073/pnas.022640199;
RA Wang J., Ortiz-Maldonado M., Entsch B., Massey V., Ballou D., Gatti D.L.;
RT "Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:608-613(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF WILD-TYPE AND MUTANT GLY-45 IN
RP COMPLEX WITH SUBSTRATE AND FAD, MUTAGENESIS OF ALA-45, FUNCTION, COFACTOR,
RP AND SUBUNIT.
RX PubMed=15924424; DOI=10.1021/bi050108x;
RA Cole L.J., Gatti D.L., Entsch B., Ballou D.P.;
RT "Removal of a methyl group causes global changes in p-hydroxybenzoate
RT hydroxylase.";
RL Biochemistry 44:8047-8058(2005).
CC -!- FUNCTION: Catalyzes the incorporation of an atom of dioxygen into p-
CC hydroxybenzoate (p-OHB) to form 3,4-dihydroxybenzoate (3,4DOHB). The
CC reaction occurs in two parts: reduction of the flavin adenine
CC dinucleotide (FAD) in the enzyme by reduced nicotinamide adenine
CC dinucleotide phosphate (NADPH) in response to binding p-hydroxybenzoate
CC to the enzyme and oxidation of reduced FAD with oxygen to form a
CC hydroperoxide, which then oxygenates p-hydroxybenzoate.
CC {ECO:0000269|PubMed:10600126, ECO:0000269|PubMed:11805318,
CC ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:1910043,
CC ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
CC ECO:0000269|PubMed:8555229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate
CC + H2O + NADP(+); Xref=Rhea:RHEA:19477, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.2; Evidence={ECO:0000269|PubMed:1910043};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
CC ECO:0000269|PubMed:1910043, ECO:0000269|PubMed:7939628,
CC ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11805318,
CC ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628,
CC ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229};
CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC hydroxylation; 3,4-dihydroxybenzoate from benzoate: step 2/2.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10600126,
CC ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
CC ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
CC ECO:0000269|PubMed:8555229}.
CC -!- MISCELLANEOUS: Controlled catalysis is achieved by movement of the
CC flavin and protein between three conformations: in, out and open. The
CC open conformation is important for substrate binding and product
CC release, the in conformation for reaction with oxygen and
CC hydroxylation, and the out conformation for the reduction of FAD by
CC NADPH. {ECO:0000269|PubMed:8555229}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family.
CC {ECO:0000305}.
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DR EMBL; M23173; AAA88455.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03636.1; -; Genomic_DNA.
DR PIR; JT0384; WHPSBA.
DR RefSeq; NP_248938.1; NC_002516.2.
DR RefSeq; WP_003112685.1; NZ_QZGE01000024.1.
DR PDB; 1D7L; X-ray; 2.20 A; A=1-394.
DR PDB; 1DOB; X-ray; 2.00 A; A=1-394.
DR PDB; 1DOC; X-ray; 2.00 A; A=1-394.
DR PDB; 1DOD; X-ray; 2.10 A; A=1-394.
DR PDB; 1DOE; X-ray; 2.30 A; A=1-394.
DR PDB; 1IUS; X-ray; 2.20 A; A=1-394.
DR PDB; 1IUT; X-ray; 2.00 A; A=1-394.
DR PDB; 1IUU; X-ray; 2.00 A; A=1-394.
DR PDB; 1IUV; X-ray; 2.50 A; A=1-394.
DR PDB; 1IUW; X-ray; 2.00 A; A=1-394.
DR PDB; 1IUX; X-ray; 2.00 A; A=1-394.
DR PDB; 1K0I; X-ray; 1.80 A; A=1-394.
DR PDB; 1K0J; X-ray; 2.20 A; A=1-394.
DR PDB; 1K0L; X-ray; 2.00 A; A=1-394.
DR PDB; 1PXA; X-ray; 2.30 A; A=1-394.
DR PDB; 1PXB; X-ray; 2.30 A; A=1-394.
DR PDB; 1PXC; X-ray; 2.10 A; A=1-394.
DR PDB; 1YKJ; X-ray; 2.00 A; A/B=1-394.
DR PDB; 6JU1; X-ray; 1.60 A; A=1-394.
DR PDBsum; 1D7L; -.
DR PDBsum; 1DOB; -.
DR PDBsum; 1DOC; -.
DR PDBsum; 1DOD; -.
DR PDBsum; 1DOE; -.
DR PDBsum; 1IUS; -.
DR PDBsum; 1IUT; -.
DR PDBsum; 1IUU; -.
DR PDBsum; 1IUV; -.
DR PDBsum; 1IUW; -.
DR PDBsum; 1IUX; -.
DR PDBsum; 1K0I; -.
DR PDBsum; 1K0J; -.
DR PDBsum; 1K0L; -.
DR PDBsum; 1PXA; -.
DR PDBsum; 1PXB; -.
DR PDBsum; 1PXC; -.
DR PDBsum; 1YKJ; -.
DR PDBsum; 6JU1; -.
DR AlphaFoldDB; P20586; -.
DR SMR; P20586; -.
DR STRING; 287.DR97_3204; -.
DR DrugBank; DB02839; 2,4-Dihydroxybenzoic Acid.
DR DrugBank; DB04242; 4-hydroxybenzoic acid.
DR DrugBank; DB03482; 8-demethyl-8-dimethylamino-flavin-adenine-dinucleotide.
DR DrugBank; DB02362; Aminobenzoic acid.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR PaxDb; P20586; -.
DR EnsemblBacteria; AAG03636; AAG03636; PA0247.
DR GeneID; 882128; -.
DR KEGG; pae:PA0247; -.
DR PATRIC; fig|208964.12.peg.257; -.
DR PseudoCAP; PA0247; -.
DR HOGENOM; CLU_057691_0_0_6; -.
DR InParanoid; P20586; -.
DR OMA; VVEPMQY; -.
DR PhylomeDB; P20586; -.
DR BioCyc; PAER208964:G1FZ6-249-MON; -.
DR BRENDA; 1.14.13.2; 5087.
DR UniPathway; UPA00156; UER00257.
DR EvolutionaryTrace; P20586; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0106356; F:4-hydroxybenzoate 3-monooxygenase [NADPH] activity; IEA:RHEA.
DR GO; GO:0018659; F:4-hydroxybenzoate 3-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012733; HB_mOase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02360; pbenz_hydroxyl; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..394
FT /note="p-hydroxybenzoate hydroxylase"
FT /id="PRO_0000058381"
FT BINDING 13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 42..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 102
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 212..214
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:15924424, ECO:0000269|PubMed:7939628,
FT ECO:0000269|PubMed:8312276, ECO:0000269|PubMed:8555229"
FT BINDING 293
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT BINDING 299..300
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10600126,
FT ECO:0000269|PubMed:11805318, ECO:0000269|PubMed:15924424,
FT ECO:0000269|PubMed:7939628, ECO:0000269|PubMed:8312276,
FT ECO:0000269|PubMed:8555229"
FT SITE 201
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:8312276"
FT SITE 385
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000269|PubMed:8312276"
FT MUTAGEN 45
FT /note="A->G: The positions of the substrate and the flavin
FT are not altered."
FT /evidence="ECO:0000269|PubMed:15924424"
FT MUTAGEN 201
FT /note="Y->F: Reduction of hydroxylase activity."
FT /evidence="ECO:0000269|PubMed:1910043,
FT ECO:0000269|PubMed:8312276"
FT MUTAGEN 220
FT /note="R->Q: Lower affinity for p-OHB than the wild-type."
FT /evidence="ECO:0000269|PubMed:11805318"
FT MUTAGEN 300
FT /note="N->D: The side chain of Asp300 moves away from the
FT flavin, disrupting the interactions of the carboxamide
FT group with the flavin O(2) atom, and the alpha-helix H10
FT that begins at residue 297 is displaced, altering its
FT dipole interactions with the flavin ring."
FT /evidence="ECO:0000269|PubMed:8312276"
FT MUTAGEN 385
FT /note="Y->F: The positions of the substrate and the flavin
FT are not altered."
FT /evidence="ECO:0000269|PubMed:1910043,
FT ECO:0000269|PubMed:8312276"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 175..192
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 236..245
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 261..278
FT /evidence="ECO:0007829|PDB:6JU1"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 298..319
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 328..350
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 358..373
FT /evidence="ECO:0007829|PDB:6JU1"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:6JU1"
SQ SEQUENCE 394 AA; 44324 MW; 1E7232854D9EC792 CRC64;
MKTQVAIIGA GPSGLLLGQL LHKAGIDNVI LERQTPDYVL GRIRAGVLEQ GMVDLLREAG
VDRRMARDGL VHEGVEIAFA GQRRRIDLKR LSGGKTVTVY GQTEVTRDLM EAREACGATT
VYQAAEVRLH DLQGERPYVT FERDGERLRL DCDYIAGCDG FHGISRQSIP AERLKVFERV
YPFGWLGLLA DTPPVSHELI YANHPRGFAL CSQRSATRSR YYVQVPLSEK VEDWSDERFW
TELKARLPSE VAEKLVTGPS LEKSIAPLRS FVVEPMQHGR LFLAGDAAHI VPPTGAKGLN
LAASDVSTLY RLLLKAYREG RGELLERYSA ICLRRIWKAE RFSWWMTSVL HRFPDTDAFS
QRIQQTELEY YLGSEAGLAT IAENYVGLPY EEIE
