YDIB_ECOLI
ID YDIB_ECOLI Reviewed; 288 AA.
AC P0A6D5; P28244; P77647;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Quinate/shikimate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000303|PubMed:3541912};
DE EC=1.1.1.282 {ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:15596430};
DE AltName: Full=NAD-dependent shikimate 5-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000303|PubMed:3541912};
GN Name=ydiB {ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000303|PubMed:3541912};
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 67-288, FUNCTION, AND SUBUNIT.
RC STRAIN=K12;
RX PubMed=3541912; DOI=10.1042/bj2380475;
RA Duncan K., Chaudhuri S., Campbell M.S., Coggins J.R.;
RT "The overexpression and complete amino acid sequence of Escherichia coli 3-
RT dehydroquinase.";
RL Biochem. J. 238:475-483(1986).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP SER-22; TYR-39; SER-67; LYS-71; ASN-92; THR-106; ASP-107 AND GLN-262, MASS
RP SPECTROMETRY, AND SUBSTRATE SPECIFICITY.
RX PubMed=15596430; DOI=10.1074/jbc.m412028200;
RA Lindner H.A., Nadeau G., Matte A., Michel G., Menard R., Cygler M.;
RT "Site-directed mutagenesis of the active site region in the
RT quinate/shikimate 5-dehydrogenase YdiB of Escherichia coli.";
RL J. Biol. Chem. 280:7162-7169(2005).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16828913; DOI=10.1016/j.jbiotec.2006.05.007;
RA Johansson L., Liden G.;
RT "Transcriptome analysis of a shikimic acid producing strain of Escherichia
RT coli W3110 grown under carbon- and phosphate-limited conditions.";
RL J. Biotechnol. 126:528-545(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, AND
RP SUBUNIT.
RX PubMed=12624088; DOI=10.1074/jbc.m301348200;
RA Benach J., Lee I., Edstrom W., Kuzin A.P., Chiang Y., Acton T.B.,
RA Montelione G.T., Hunt J.F.;
RT "The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue
RT YdiB from Escherichia coli suggests a novel catalytic environment for an
RT NAD-dependent dehydrogenase.";
RL J. Biol. Chem. 278:19176-19182(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=12637497; DOI=10.1074/jbc.m300794200;
RA Michel G., Roszak A.W., Sauve V., Maclean J., Matte A., Coggins J.R.,
RA Cygler M., Lapthorn A.J.;
RT "Structures of shikimate dehydrogenase AroE and its paralog YdiB. A common
RT structural framework for different activities.";
RL J. Biol. Chem. 278:19463-19472(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-288 IN COMPLEX WITH NAD, AND
RP SUBUNIT.
RX PubMed=16021622; DOI=10.1002/prot.20541;
RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G.,
RA Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S.,
RA Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D.,
RA Hendle J., Huber A., Hoda K., Kearins P., Kissinger C., Laubert B.,
RA Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M.,
RA Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M.,
RA Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S.,
RA Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J.,
RA Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.;
RT "Structural analysis of a set of proteins resulting from a bacterial
RT genomics project.";
RL Proteins 60:787-796(2005).
CC -!- FUNCTION: The actual biological function of YdiB remains unclear, nor
CC is it known whether 3-dehydroshikimate or quinate represents the
CC natural substrate. Catalyzes the reversible NAD-dependent reduction of
CC both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate
CC (SA) and quinate, respectively. It can use both NAD or NADP for
CC catalysis, however it has higher catalytic efficiency with NAD.
CC {ECO:0000255|HAMAP-Rule:MF_01578, ECO:0000269|PubMed:12624088,
CC ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:15596430}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH;
CC Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751,
CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578,
CC ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:15596430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-quinate + NADP(+) = 3-dehydroquinate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18425, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751,
CC ChEBI:CHEBI:32364, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578,
CC ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:15596430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578,
CC ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:15596430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH;
CC Xref=Rhea:RHEA:17741, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.282; Evidence={ECO:0000255|HAMAP-Rule:MF_01578,
CC ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:15596430};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 uM for shikimate (at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:15596430};
CC KM=9.1 uM for quinate (at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:15596430};
CC KM=12.2 uM for NAD (with shikimate at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:15596430};
CC KM=18.4 uM for NAD (with quinate at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:15596430};
CC KM=20 uM for shikimate (with NAD at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC KM=41 uM for quinate (with NAD at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC KM=87 uM for NAD (with shikimate at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC KM=100 uM for NADP (with shikimate at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC KM=116 uM for NAD (with quinate at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC KM=120 uM for shikimate (with NADP at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC KM=500 uM for NADP (with quinate at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC KM=555 uM for quinate (with NADP at pH 9 and 20 degrees Celsius)
CC {ECO:0000269|PubMed:12637497};
CC Note=kcat is 91 sec(-1) for dehydrogenase activity with shikimate (at
CC pH 9 and 20 degrees Celsius). kcat is 113 sec(-1) for dehydrogenase
CC activity with quinate (at pH 9 and 20 degrees Celsius). kcat is 105
CC sec(-1) for dehydrogenase activity with NAD (with shikinate at pH 9
CC and 20 degrees Celsius). kcat is 142 sec(-1) for dehydrogenase
CC activity with NAD (with quinate at pH 9 and 20 degrees Celsius).;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000255|HAMAP-Rule:MF_01578}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01578,
CC ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497,
CC ECO:0000269|PubMed:16021622, ECO:0000269|PubMed:3541912}.
CC -!- INTERACTION:
CC P0A6D5; P25894: loiP; NbExp=2; IntAct=EBI-560638, EBI-560654;
CC -!- INDUCTION: Induced under carbon limitation but not under phosphate
CC limitation. {ECO:0000269|PubMed:16828913}.
CC -!- MASS SPECTROMETRY: Mass=31361; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:15596430};
CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01578}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA27848.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00096; AAC74762.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15449.1; -; Genomic_DNA.
DR EMBL; X04306; CAA27848.1; ALT_FRAME; Genomic_DNA.
DR PIR; D64927; D64927.
DR RefSeq; NP_416207.1; NC_000913.3.
DR RefSeq; WP_000383469.1; NZ_SSZK01000001.1.
DR PDB; 1NPD; X-ray; 2.30 A; A/B=1-288.
DR PDB; 1O9B; X-ray; 2.50 A; A/B=1-288.
DR PDB; 1VI2; X-ray; 2.10 A; A/B=2-288.
DR PDBsum; 1NPD; -.
DR PDBsum; 1O9B; -.
DR PDBsum; 1VI2; -.
DR AlphaFoldDB; P0A6D5; -.
DR SMR; P0A6D5; -.
DR BioGRID; 4263505; 7.
DR DIP; DIP-47967N; -.
DR IntAct; P0A6D5; 3.
DR STRING; 511145.b1692; -.
DR PaxDb; P0A6D5; -.
DR PRIDE; P0A6D5; -.
DR EnsemblBacteria; AAC74762; AAC74762; b1692.
DR EnsemblBacteria; BAA15449; BAA15449; BAA15449.
DR GeneID; 946200; -.
DR KEGG; ecj:JW1682; -.
DR KEGG; eco:b1692; -.
DR PATRIC; fig|1411691.4.peg.566; -.
DR EchoBASE; EB1216; -.
DR eggNOG; COG0169; Bacteria.
DR HOGENOM; CLU_044063_4_4_6; -.
DR InParanoid; P0A6D5; -.
DR OMA; SIFARND; -.
DR PhylomeDB; P0A6D5; -.
DR BioCyc; EcoCyc:EG11234-MON; -.
DR BioCyc; MetaCyc:EG11234-MON; -.
DR BRENDA; 1.1.1.25; 2026.
DR BRENDA; 1.1.1.282; 2026.
DR SABIO-RK; P0A6D5; -.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; P0A6D5; -.
DR PRO; PR:P0A6D5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030266; F:quinate 3-dehydrogenase (NAD+) activity; IDA:EcoCyc.
DR GO; GO:0052733; F:quinate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0052734; F:shikimate 3-dehydrogenase (NAD+) activity; IDA:EcoCyc.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:EcoCyc.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR GO; GO:0019632; P:shikimate metabolic process; IBA:GO_Central.
DR HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR HAMAP; MF_01578; Shikimate_DH_YdiB; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR022872; Quinate/Shikimate_DH.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16021622"
FT CHAIN 2..288
FT /note="Quinate/shikimate dehydrogenase"
FT /id="PRO_0000136069"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578"
FT BINDING 132..135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497,
FT ECO:0000269|PubMed:16021622"
FT BINDING 155..158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497,
FT ECO:0000269|PubMed:16021622"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497,
FT ECO:0000269|PubMed:16021622"
FT BINDING 232..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497,
FT ECO:0000269|PubMed:16021622"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01578,
FT ECO:0000269|PubMed:12624088, ECO:0000269|PubMed:12637497,
FT ECO:0000269|PubMed:16021622"
FT MUTAGEN 22
FT /note="S->A: Kinetically unchanged as compared with the
FT wild-type."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 39
FT /note="Y->F: Kinetically unchanged as compared with the
FT wild-type."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 67
FT /note="S->A: Reduces activity towards quinate about 6-fold,
FT but has a little effect on shikimate conversion."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 71
FT /note="K->A: 3200-fold decrease in the affinity for
FT quinate. 170-fold decrease in the affinity for shikimate."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 71
FT /note="K->G: 10-fold greater reduction in catalytic
FT efficiency is observed with quinate than with shikimate."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 92
FT /note="N->A: Alters protein structure. Loss of activity for
FT both substrates."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 106
FT /note="T->A: 2000-fold decrease in the affinity for
FT quinate. 70-fold decrease in the affinity for shikimate.
FT 10-fold greater reduction in catalytic efficiency is
FT observed with quinate than with shikimate."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 107
FT /note="D->A: Loss of activity towards quinate. 20000-fold
FT decrease in the affinity for shikimate."
FT /evidence="ECO:0000269|PubMed:15596430"
FT MUTAGEN 262
FT /note="Q->A: 3-fold reduction in catalytic efficiency for
FT both substrates."
FT /evidence="ECO:0000269|PubMed:15596430"
FT STRAND 8..15
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1VI2"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 134..145
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:1VI2"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1VI2"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:1VI2"
FT HELIX 277..284
FT /evidence="ECO:0007829|PDB:1VI2"
SQ SEQUENCE 288 AA; 31228 MW; C3D1415E03820A5A CRC64;
MDVTAKYELI GLMAYPIRHS LSPEMQNKAL EKAGLPFTYM AFEVDNDSFP GAIEGLKALK
MRGTGVSMPN KQLACEYVDE LTPAAKLVGA INTIVNDDGY LRGYNTDGTG HIRAIKESGF
DIKGKTMVLL GAGGASTAIG AQGAIEGLKE IKLFNRRDEF FDKALAFAQR VNENTDCVVT
VTDLADQQAF AEALASADIL TNGTKVGMKP LENESLVNDI SLLHPGLLVT ECVYNPHMTK
LLQQAQQAGC KTIDGYGMLL WQGAEQFTLW TGKDFPLEYV KQVMGFGA
