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   04-NOV-2026, entry version 186.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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 IN COMPLEX WITH IRON; 2-OXOGLUTARATE AND TAURINE,
RP   CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND HYDROXYLATION AT TRP-128;
RP   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 IN COMPLEX WITH IRON; 2-OXOGLUTARATE AND TAURINE,
RP   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=taurine + 2-oxoglutarate + O2 = aminoacetaldehyde + sulfite +
CC         succinate + CO2 + H(+); 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 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
CC         1,3-dioxo-2-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_CP009789.1.
DR   PDB; 1GQW; X-ray; 3.00 A; A/B=1-283.
DR   PDB; 1GY9; X-ray; 2.50 A; A/B=1-283.
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   SMR; P37610; -.
DR   BioGRID; 4259830; 18.
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   STRING; 511145.b0368; -.
DR   DrugBank; DB01956; Taurine.
DR   PaxDb; 511145-b0368; -.
DR   EnsemblBacteria; AAC73471; AAC73471; b0368.
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; AAMKYNY; -.
DR   OrthoDB; 581608at2; -.
DR   PhylomeDB; P37610; -.
DR   BioCyc; EcoCyc:MONOMER0-147; -.
DR   BioCyc; MetaCyc:MONOMER0-147; -.
DR   BRENDA; 1.14.11.17; 2026.
DR   SABIO-RK; P37610; -.
DR   UniPathway; UPA00336; UER00542.
DR   EvolutionaryTrace; P37610; -.
DR   PRO; PR:P37610; -.
DR   AbasyAtlas; P37610; -.
DR   FunFam; 3.60.130.10:FF:000002; Alpha-ketoglutarate-dependent taurine dioxygenase; 1.
DR   Gene3D; 3.60.130.10; Clavaminate synthase-like; 1.
DR   InterPro; IPR051323; AtsK-like.
DR   InterPro; IPR042098; GlaH-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   PANTHER; PTHR30468; ALPHA-KETOGLUTARATE-DEPENDENT SULFONATE DIOXYGENASE; 1.
DR   PANTHER; PTHR30468:SF1; ALPHA-KETOGLUTARATE-DEPENDENT SULFONATE DIOXYGENASE; 1.
DR   Pfam; PF02668; TauD; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   NCBIfam; NF007104; tauD; 1.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:1990205; C:taurine dioxygenase complex; IDA:EcoCyc.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IPI:EcoCyc.
DR   GO; GO:0000908; F:taurine dioxygenase activity; IDA:EcoliWiki.
DR   GO; GO:0051289; P:protein homotetramerization; IPI:EcoCyc.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IMP:EcoliWiki.
DR   GO; GO:0019529; P:taurine catabolic process; IDA:ComplexPortal.
DR   Proteomes; UP000000625; Chromosome.
DR   AlphaFoldDB; P37610; -.
DR   FunCoup; P37610; 519.
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..158
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
//