TAUD_ECOLI
ID TAUD_ECOLI Reviewed; 283 AA.
AC P37610; P77797; Q2MC57; Q47540;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Alpha-ketoglutarate-dependent taurine dioxygenase {ECO:0000303|PubMed:9287300};
DE EC=1.14.11.17 {ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810, ECO:0000269|PubMed:9287300};
DE AltName: Full=2-aminoethanesulfonate dioxygenase;
DE AltName: Full=Sulfate starvation-induced protein 3;
DE Short=SSI3;
GN Name=tauD; Synonyms=ssiD, yaiG; OrderedLocusNames=b0368, JW0360;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=K12;
RX PubMed=8808933; DOI=10.1128/jb.178.18.5438-5446.1996;
RA van der Ploeg J.R., Weiss M.A., Saller E., Nashimoto H., Saito N.,
RA Kertesz M.A., Leisinger T.;
RT "Identification of sulfate starvation-regulated genes in Escherichia coli:
RT a gene cluster involved in the utilization of taurine as a sulfur source.";
RL J. Bacteriol. 178:5438-5446(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 237-283.
RC STRAIN=K12;
RX PubMed=2656410; DOI=10.1016/0378-1119(89)90394-6;
RA Li J.-M., Russell C.S., Cosloy S.D.;
RT "The structure of the Escherichia coli hemB gene.";
RL Gene 75:177-184(1989).
RN [6]
RP PROTEIN SEQUENCE OF 2-11; 42-46 AND 59-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8774726; DOI=10.1111/j.1432-1033.1996.0773u.x;
RA Quadroni M., Staudenmann W., Kertesz M.A., James P.;
RT "Analysis of global responses by protein and peptide fingerprinting of
RT proteins isolated by two-dimensional gel electrophoresis. Application to
RT the sulfate-starvation response of Escherichia coli.";
RL Eur. J. Biochem. 239:773-781(1996).
RN [7]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBUNIT, AND INDUCTION.
RX PubMed=9287300; DOI=10.1074/jbc.272.37.23031;
RA Eichhorn E., van der Ploeg J.R., Kertesz M.A., Leisinger T.;
RT "Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from
RT Escherichia coli.";
RL J. Biol. Chem. 272:23031-23036(1997).
RN [9]
RP BIOTECHNOLOGY.
RC STRAIN=K12;
RX PubMed=22595347; DOI=10.1016/j.ab.2012.04.030;
RA Matsuda M., Asano Y.;
RT "A simple assay of taurine concentrations in food and biological samples
RT using taurine dioxygenase.";
RL Anal. Biochem. 427:121-123(2012).
RN [10]
RP SUBUNIT.
RX PubMed=22221834; DOI=10.1111/j.1742-4658.2012.08473.x;
RA Knauer S.H., Hartl-Spiegelhauer O., Schwarzinger S., Hanzelmann P.,
RA Dobbek H.;
RT "The Fe(II)/alpha-ketoglutarate-dependent taurine dioxygenases from
RT Pseudomonas putida and Escherichia coli are tetramers.";
RL FEBS J. 279:816-831(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH IRON; 2-OXOGLUTARATE
RP AND TAURINE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND HYDROXYLATION AT
RP TRP-128; TRP-240 AND TRP-248.
RX PubMed=11955067; DOI=10.1021/bi016014e;
RA Elkins J.M., Ryle M.J., Clifton I.J., Dunning Hotopp J.C., Lloyd J.S.,
RA Burzlaff N.I., Baldwin J.E., Hausinger R.P., Roach P.L.;
RT "X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate
RT dioxygenase complexed to ferrous iron and substrates.";
RL Biochemistry 41:5185-5192(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH IRON; 2-OXOGLUTARATE
RP AND TAURINE, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
RX PubMed=12741810; DOI=10.1021/bi0341096;
RA O'Brien J.R., Schuller D.J., Yang V.S., Dillard B.D., Lanzilotta W.N.;
RT "Substrate-induced conformational changes in Escherichia coli
RT taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric
RT structure.";
RL Biochemistry 42:5547-5554(2003).
CC -!- FUNCTION: Catalyzes the alpha-ketoglutarate-dependent hydroxylation of
CC taurine yielding sulfite and aminoacetaldehyde after decomposition of
CC an unstable intermediate (PubMed:9287300). Is required for the
CC utilization of taurine (2-aminoethanesulfonate) as an alternative
CC sulfur source for growth in the absence of sulfate (PubMed:8808933). To
CC a lesser extent, pentanesulfonate, 3-(N-morpholino)propanesulfonate and
CC 1,3-dioxo-2-isoindolineethanesulfonate are also desulfonated by this
CC enzyme in vitro; however, desulfonation by TauD of organosulfonates
CC other than taurine seem to be of little or no importance for sulfur
CC metabolism in vivo (PubMed:9287300). {ECO:0000269|PubMed:8808933,
CC ECO:0000269|PubMed:9287300}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O2 + taurine = aminoacetaldehyde + CO2 + H(+)
CC + succinate + sulfite; Xref=Rhea:RHEA:15909, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:30031, ChEBI:CHEBI:58213,
CC ChEBI:CHEBI:507393; EC=1.14.11.17;
CC Evidence={ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810,
CC ECO:0000269|PubMed:9287300, ECO:0000305|PubMed:8808933};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15910;
CC Evidence={ECO:0000269|PubMed:8808933};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:11955067, ECO:0000269|PubMed:12741810,
CC ECO:0000269|PubMed:9287300};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:11955067,
CC ECO:0000269|PubMed:12741810};
CC -!- ACTIVITY REGULATION: Activated by ascorbate and inhibited by divalent
CC metal ions such as zinc, copper and cobalt.
CC {ECO:0000269|PubMed:9287300}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 uM for taurine (at pH 6.9) {ECO:0000269|PubMed:9287300};
CC KM=11 uM for 2-oxoglutarate (at pH 6.9) {ECO:0000269|PubMed:9287300};
CC KM=1490 uM for butanesulfonate (at pH 6.9)
CC {ECO:0000269|PubMed:9287300};
CC KM=590 uM for pentanesulfonate (at pH 6.9)
CC {ECO:0000269|PubMed:9287300};
CC KM=1510 uM for hexanesulfonate (at pH 6.9)
CC {ECO:0000269|PubMed:9287300};
CC KM=145 uM for 3-(N-morpholino)propanesulfonate (at pH 6.9)
CC {ECO:0000269|PubMed:9287300};
CC KM=485 uM for 1,3-dioxo-2-isoindolineethanesulfonate (at pH 6.9)
CC {ECO:0000269|PubMed:9287300};
CC Vmax=4.1 umol/min/mg enzyme with taurine as substrate (at pH 6.9)
CC {ECO:0000269|PubMed:9287300};
CC Vmax=1.3 umol/min/mg enzyme with butanesulfonate as substrate (at pH
CC 6.9) {ECO:0000269|PubMed:9287300};
CC Vmax=1.9 umol/min/mg enzyme with pentanesulfonate as substrate (at pH
CC 6.9) {ECO:0000269|PubMed:9287300};
CC Vmax=2.2 umol/min/mg enzyme with hexanesulfonate as substrate (at pH
CC 6.9) {ECO:0000269|PubMed:9287300};
CC Vmax=2.0 umol/min/mg enzyme with 3-(N-morpholino)propanesulfonate as
CC substrate (at pH 6.9) {ECO:0000269|PubMed:9287300};
CC Vmax=3.8 umol/min/mg enzyme with 1,3-dioxo-2-
CC isoindolineethanesulfonate as substrate (at pH 6.9)
CC {ECO:0000269|PubMed:9287300};
CC pH dependence:
CC Optimum pH is 6.9. {ECO:0000269|PubMed:9287300};
CC -!- PATHWAY: Organosulfur degradation; taurine degradation via aerobic
CC pathway; aminoacetaldehyde and sulfite from taurine: step 1/1.
CC {ECO:0000269|PubMed:8808933}.
CC -!- SUBUNIT: Homodimer (PubMed:11955067, PubMed:12741810, PubMed:9287300).
CC Was later shown to be a homotetramer arranged as a dimer of two dimers
CC (PubMed:22221834). {ECO:0000269|PubMed:11955067,
CC ECO:0000269|PubMed:12741810, ECO:0000269|PubMed:22221834,
CC ECO:0000269|PubMed:9287300}.
CC -!- INDUCTION: Is only expressed during growth in the absence of sulfate or
CC cysteine. {ECO:0000269|PubMed:8808933, ECO:0000269|PubMed:9287300}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene leads to a loss of the
CC ability to utilize taurine as a source of sulfur, but does not affect
CC the utilization of a range of other aliphatic sulfonates as sulfur
CC sources. {ECO:0000269|PubMed:8808933}.
CC -!- BIOTECHNOLOGY: Taurine dioxygenase can be used for enzymatic
CC determination of taurine concentration in food quality control,
CC biological research, and medical diagnosis.
CC {ECO:0000269|PubMed:22595347}.
CC -!- SIMILARITY: Belongs to the TfdA dioxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=M24488; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D85613; BAA12841.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18091.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73471.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76149.1; -; Genomic_DNA.
DR EMBL; M24488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S78607; H64764.
DR RefSeq; NP_414902.1; NC_000913.3.
DR RefSeq; WP_000004027.1; NZ_SSZK01000009.1.
DR PDB; 1GQW; X-ray; 3.00 A; A/B=2-283.
DR PDB; 1GY9; X-ray; 2.50 A; A/B=2-283.
DR PDB; 1OS7; X-ray; 2.50 A; A/B/C/D=1-283.
DR PDB; 1OTJ; X-ray; 1.90 A; A/B/C/D=1-283.
DR PDB; 6EDH; X-ray; 1.73 A; A/B=1-283.
DR PDBsum; 1GQW; -.
DR PDBsum; 1GY9; -.
DR PDBsum; 1OS7; -.
DR PDBsum; 1OTJ; -.
DR PDBsum; 6EDH; -.
DR AlphaFoldDB; P37610; -.
DR SMR; P37610; -.
DR BioGRID; 4259830; 13.
DR ComplexPortal; CPX-2120; Taurine dioxygenase complex, tetrameric.
DR ComplexPortal; CPX-3190; Taurine dioxygenase complex, dimeric.
DR DIP; DIP-10966N; -.
DR IntAct; P37610; 4.
DR MINT; P37610; -.
DR STRING; 511145.b0368; -.
DR DrugBank; DB01956; Taurine.
DR PaxDb; P37610; -.
DR PRIDE; P37610; -.
DR EnsemblBacteria; AAC73471; AAC73471; b0368.
DR EnsemblBacteria; BAE76149; BAE76149; BAE76149.
DR GeneID; 66671330; -.
DR GeneID; 945021; -.
DR KEGG; ecj:JW0360; -.
DR KEGG; eco:b0368; -.
DR PATRIC; fig|1411691.4.peg.1911; -.
DR EchoBASE; EB2322; -.
DR eggNOG; COG2175; Bacteria.
DR HOGENOM; CLU_036005_2_1_6; -.
DR InParanoid; P37610; -.
DR OMA; FVDAYPK; -.
DR PhylomeDB; P37610; -.
DR BioCyc; EcoCyc:MON0-147; -.
DR BioCyc; MetaCyc:MON0-147; -.
DR BRENDA; 1.14.11.17; 2026.
DR SABIO-RK; P37610; -.
DR UniPathway; UPA00336; UER00542.
DR EvolutionaryTrace; P37610; -.
DR PRO; PR:P37610; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:1990205; C:taurine dioxygenase complex; IDA:EcoCyc.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0000908; F:taurine dioxygenase activity; IDA:EcoliWiki.
DR GO; GO:0006790; P:sulfur compound metabolic process; IMP:EcoliWiki.
DR GO; GO:0019529; P:taurine catabolic process; IDA:ComplexPortal.
DR Gene3D; 3.60.130.10; -; 1.
DR InterPro; IPR042098; TauD-like_sf.
DR InterPro; IPR003819; TauD/TfdA-like.
DR Pfam; PF02668; TauD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Direct protein sequencing; Hydroxylation; Iron;
KW Metal-binding; Oxidoreductase; Reference proteome; Vitamin C.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8774726"
FT CHAIN 2..283
FT /note="Alpha-ketoglutarate-dependent taurine dioxygenase"
FT /id="PRO_0000194016"
FT BINDING 70
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 73
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 95
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 99
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 101
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 102
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 126
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 255
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 255
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 266
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 270
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT BINDING 270
FT /ligand="taurine"
FT /ligand_id="ChEBI:CHEBI:507393"
FT /evidence="ECO:0000269|PubMed:11955067,
FT ECO:0000269|PubMed:12741810"
FT MOD_RES 128
FT /note="3-hydroxytryptophan; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11955067"
FT MOD_RES 240
FT /note="3-hydroxytryptophan; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11955067"
FT MOD_RES 248
FT /note="3-hydroxytryptophan; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11955067"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:6EDH"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:6EDH"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6EDH"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:6EDH"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6EDH"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:6EDH"
SQ SEQUENCE 283 AA; 32410 MW; 7ADEB0CDC9CEEB57 CRC64;
MSERLSITPL GPYIGAQISG ADLTRPLSDN QFEQLYHAVL RHQVVFLRDQ AITPQQQRAL
AQRFGELHIH PVYPHAEGVD EIIVLDTHND NPPDNDNWHT DVTFIETPPA GAILAAKELP
STGGDTLWTS GIAAYEALSV PFRQLLSGLR AEHDFRKSFP EYKYRKTEEE HQRWREAVAK
NPPLLHPVVR THPVSGKQAL FVNEGFTTRI VDVSEKESEA LLSFLFAHIT KPEFQVRWRW
QPNDIAIWDN RVTQHYANAD YLPQRRIMHR ATILGDKPFY RAG
