BADH_SPIOL
ID BADH_SPIOL Reviewed; 497 AA.
AC P17202; A0A0K9R405; B9VRI5; P93555; Q8H1B4;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Aminoaldehyde dehydrogenase BADH {ECO:0000305};
DE EC=1.2.1.- {ECO:0000269|PubMed:22345508};
DE AltName: Full=4-trimethylammoniobutyraldehyde dehydrogenase BADH {ECO:0000305};
DE EC=1.2.1.47 {ECO:0000269|PubMed:22345508};
DE AltName: Full=Aminobutyraldehyde dehydrogenase BADH {ECO:0000305};
DE EC=1.2.1.19 {ECO:0000269|PubMed:22345508};
DE AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000305};
DE Short=SoBADH {ECO:0000303|PubMed:22345508};
DE EC=1.2.1.8 {ECO:0000269|PubMed:22345508};
GN Name=BADH {ECO:0000303|PubMed:2320587};
GN ORFNames=SOVF_114720 {ECO:0000312|EMBL:KNA13664.1};
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP INDUCTION BY SALT STRESS.
RC STRAIN=cv. Savoy hybrid 612;
RX PubMed=2320587; DOI=10.1073/pnas.87.7.2745;
RA Weretilnyk E.A., Hanson A.D.;
RT "Molecular cloning of a plant betaine-aldehyde dehydrogenase, an enzyme
RT implicated in adaptation to salinity and drought.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2745-2749(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shu W., Ai W., Chen S.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang D., Zhang N., Si H.J.;
RT "Isolation and identification of betaine aldehyde dehydrogenase (BADH) gene
RT from spinach (Spinacia oleracea L.).";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li S., Yang X.;
RT "Spinacia oleracea betaine aldehyde dehydrogenase (BADH) mRNA.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Allahi S., Sohani M.M., Hassani H.;
RT "Functional characterization of betainealdehyde dehydrogenase (BADH)
RT transgene in Medicago truncatula L.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Viroflay; TISSUE=Leaf;
RX PubMed=24352233; DOI=10.1038/nature12817;
RA Dohm J.C., Minoche A.E., Holtgraewe D., Capella-Gutierrez S.,
RA Zakrzewski F., Tafer H., Rupp O., Soerensen T.R., Stracke R., Reinhardt R.,
RA Goesmann A., Kraft T., Schulz B., Stadler P.F., Schmidt T., Gabaldon T.,
RA Lehrach H., Weisshaar B., Himmelbauer H.;
RT "The genome of the recently domesticated crop plant sugar beet (Beta
RT vulgaris).";
RL Nature 505:546-549(2014).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ALA-441.
RX PubMed=24884441; DOI=10.1186/1471-2229-14-149;
RA Munoz-Clares R.A., Riveros-Rosas H., Garza-Ramos G., Gonzalez-Segura L.,
RA Mujica-Jimenez C., Julian-Sanchez A.;
RT "Exploring the evolutionary route of the acquisition of betaine aldehyde
RT dehydrogenase activity by plant ALDH10 enzymes: implications for the
RT synthesis of the osmoprotectant glycine betaine.";
RL BMC Plant Biol. 14:149-149(2014).
RN [8]
RP ACTIVITY REGULATION.
RX PubMed=30928398; DOI=10.1016/j.cbi.2019.03.024;
RA Munoz-Clares R.A., Casanova-Figueroa K.;
RT "The importance of assessing aldehyde substrate inhibition for the correct
RT determination of kinetic parameters and mechanisms: the case of the ALDH
RT enzymes.";
RL Chem. Biol. Interact. 305:86-97(2019).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-496 IN COMPLEX WITH NAD AND
RP POTASSIUM IONS, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF TYR-160; TRP-167; TRP-285;
RP ALA-441 AND TRP-456.
RX PubMed=22345508; DOI=10.1104/pp.112.194514;
RA Diaz-Sanchez A.G., Gonzalez-Segura L., Mujica-Jimenez C., Rudino-Pinera E.,
RA Montiel C., Martinez-Castilla L.P., Munoz-Clares R.A.;
RT "Amino acid residues critical for the specificity for betaine aldehyde of
RT the plant ALDH10 isoenzyme involved in the synthesis of glycine betaine.";
RL Plant Physiol. 158:1570-1582(2012).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) IN COMPLEX WITH POTASSIUM IONS,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF CYS-450.
RX PubMed=26792760; DOI=10.1042/bj20151084;
RA Zarate-Romero A., Murillo-Melo D.S., Mujica-Jimenez C., Montiel C.,
RA Munoz-Clares R.A.;
RT "Reversible, partial inactivation of plant betaine aldehyde dehydrogenase
RT by betaine aldehyde: mechanism and possible physiological implications.";
RL Biochem. J. 473:873-885(2016).
CC -!- FUNCTION: Dehydrogenase innvolved in glycine betaine biosynthesis
CC (PubMed:2320587, PubMed:24884441, PubMed:22345508). Metabolizes and
CC detoxifies aldehyde products of polyamine degradation to non-toxic
CC amino acids (Probable). Catalyzes the oxidation of betaine aldehyde to
CC glycine betaine (PubMed:24884441, PubMed:22345508). Catalyzes the
CC oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and
CC beta-alanine, respectively (PubMed:22345508).
CC {ECO:0000269|PubMed:22345508, ECO:0000269|PubMed:2320587,
CC ECO:0000269|PubMed:24884441, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000269|PubMed:22345508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000269|PubMed:22345508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-aminopropanal + H2O + NAD(+) = beta-alanine + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:30695, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57966,
CC ChEBI:CHEBI:58374; Evidence={ECO:0000269|PubMed:22345508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30696;
CC Evidence={ECO:0000269|PubMed:22345508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(trimethylamino)butanal + H2O + NAD(+) = 4-
CC (trimethylamino)butanoate + 2 H(+) + NADH; Xref=Rhea:RHEA:17985,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16244,
CC ChEBI:CHEBI:18020, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.47;
CC Evidence={ECO:0000269|PubMed:22345508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17986;
CC Evidence={ECO:0000269|PubMed:22345508};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8;
CC Evidence={ECO:0000269|PubMed:22345508};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000269|PubMed:22345508};
CC -!- ACTIVITY REGULATION: Is reversibly and partially inactivated by betaine
CC aldehyde in the absence of NAD(+) in a time- and concentration-
CC dependent mode. {ECO:0000269|PubMed:26792760,
CC ECO:0000269|PubMed:30928398}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=69 uM for betaine aldehyde {ECO:0000269|PubMed:22345508};
CC KM=5.5 uM for 4-aminobutanal {ECO:0000269|PubMed:22345508};
CC KM=2.6 uM for 3-aminopropanal {ECO:0000269|PubMed:22345508};
CC KM=3.6 uM for 4-(trimethylamino)butanal
CC {ECO:0000269|PubMed:22345508};
CC Vmax=5 umol/min/mg enzyme with beta aldehyde as substrate
CC {ECO:0000269|PubMed:22345508};
CC Vmax=0.58 umol/min/mg enzyme with 4-aminobutanal as substrate
CC {ECO:0000269|PubMed:22345508};
CC Vmax=0.7 umol/min/mg enzyme with 3-aminopropanal as substrate
CC {ECO:0000269|PubMed:22345508};
CC Vmax=1.2 umol/min/mg enzyme with 4-(trimethylamino)butanal as
CC substrate {ECO:0000269|PubMed:22345508};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000305}.
CC -!- SUBUNIT: Forms homodimers. {ECO:0000269|PubMed:22345508}.
CC -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:2320587}.
CC -!- MISCELLANEOUS: The catalytic activity of the dimeric betaine aldehyde
CC (BADH) from spinach does not require potassium ion as cofactor,
CC contrary to the tetrameric BADH from Pseudomonas aeruginosa (AC
CC Q9HTJ1), although both enzymes contain potassium-binding sites.
CC {ECO:0000269|PubMed:26792760}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M31480; AAA34025.1; -; mRNA.
DR EMBL; U69142; AAB41696.1; -; Genomic_DNA.
DR EMBL; AY156694; AAN52929.1; -; mRNA.
DR EMBL; FJ595952; ACM67311.1; -; mRNA.
DR EMBL; KQ152304; KNA13664.1; -; Genomic_DNA.
DR EMBL; KU743399; AOA60050.1; -; mRNA.
DR PIR; A35994; A35994.
DR PIR; T51173; T51173.
DR PDB; 4A0M; X-ray; 2.30 A; A/B/C/D=1-496.
DR PDB; 4V37; X-ray; 2.10 A; A/B/C/D=1-497.
DR PDB; 4V3F; X-ray; 2.00 A; A/B/C/D=1-497.
DR PDB; 5A2D; X-ray; 1.98 A; A/B/C/D=1-497.
DR PDBsum; 4A0M; -.
DR PDBsum; 4V37; -.
DR PDBsum; 4V3F; -.
DR PDBsum; 5A2D; -.
DR AlphaFoldDB; P17202; -.
DR SMR; P17202; -.
DR STRING; 3562.A0A0K9R405; -.
DR PRIDE; P17202; -.
DR OrthoDB; 153834at2759; -.
DR BRENDA; 1.2.1.8; 5812.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000054095; Unassembled WGS sequence.
DR GO; GO:0047105; F:4-trimethylammoniobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IDA:UniProtKB.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IDA:UniProtKB.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Metal-binding; NAD;
KW Oxidoreductase; Potassium; Reference proteome.
FT CHAIN 1..497
FT /note="Aminoaldehyde dehydrogenase BADH"
FT /id="PRO_0000007182"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 291
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008,
FT ECO:0000305|PubMed:22345508"
FT BINDING 28
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M,
FT ECO:0007744|PDB:5A2D"
FT BINDING 96
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M,
FT ECO:0007744|PDB:5A2D"
FT BINDING 156..158
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37"
FT BINDING 182..185
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M,
FT ECO:0007744|PDB:5A2D"
FT BINDING 236..239
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37"
FT BINDING 251
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M,
FT ECO:0007744|PDB:5A2D"
FT BINDING 258
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0007744|PDB:4V37"
FT BINDING 390
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37"
FT BINDING 456
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0007744|PDB:4A0M, ECO:0007744|PDB:4V37"
FT BINDING 460
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0000269|PubMed:26792760, ECO:0007744|PDB:4A0M,
FT ECO:0007744|PDB:5A2D"
FT SITE 159
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
FT MOD_RES 8
FT /note="Blocked amino end (Arg)"
FT MUTAGEN 160
FT /note="Y->A: Decreases binding affinity for betaine
FT aldehyde; increases binding affinity for 4-
FT (trimethylamino)butanal."
FT /evidence="ECO:0000269|PubMed:22345508"
FT MUTAGEN 167
FT /note="W->A: Decreases binding affinity for betaine
FT aldehyde; increases binding affinity for 4-aminobutanal."
FT /evidence="ECO:0000269|PubMed:22345508"
FT MUTAGEN 285
FT /note="W->A: Decreases binding affinity for betaine
FT aldehyde."
FT /evidence="ECO:0000269|PubMed:22345508"
FT MUTAGEN 441
FT /note="A->I: Decreases binding affinity for betaine
FT aldehyde; increases binding affinity for 4-aminobutanal."
FT /evidence="ECO:0000269|PubMed:22345508,
FT ECO:0000269|PubMed:24884441"
FT MUTAGEN 450
FT /note="C->S: Loss of partial inactivation by betaine
FT aldehyde in the absence of NAD(+)."
FT /evidence="ECO:0000269|PubMed:26792760"
FT MUTAGEN 456
FT /note="W->A: Decreases binding affinity for betaine
FT aldehyde."
FT /evidence="ECO:0000269|PubMed:22345508"
FT CONFLICT 15
FT /note="E -> G (in Ref. 4; ACM67311)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="I -> V (in Ref. 3; AAN52929)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="C -> R (in Ref. 3; AAN52929)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="S -> F (in Ref. 2; AAB41696)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:5A2D"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 44..59
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4A0M"
FT HELIX 68..84
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 101..126
FT /evidence="ECO:0007829|PDB:5A2D"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 301..316
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 336..352
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 393..403
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 404..412
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 439..446
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:5A2D"
FT HELIX 469..476
FT /evidence="ECO:0007829|PDB:5A2D"
FT STRAND 477..485
FT /evidence="ECO:0007829|PDB:5A2D"
SQ SEQUENCE 497 AA; 54270 MW; 55088240E635B22F CRC64;
MAFPIPARQL FIDGEWREPI KKNRIPVINP STEEIIGDIP AATAEDVEVA VVAARRAFRR
NNWSATSGAH RATYLRAIAA KITEKKDHFV KLETIDSGKP FDEAVLDIDD VASCFEYFAG
QAEALDGKQK APVTLPMERF KSHVLRQPLG VVGLISPWNY PLLMATWKIA PALAAGCTAV
LKPSELASVT CLEFGEVCNE VGLPPGVLNI LTGLGPDAGA PLVSHPDVDK IAFTGSSATG
SKVMASAAQL VKPVTLELGG KSPIVVFEDV DIDKVVEWTI FGCFWTNGQI CSATSRLLVH
ESIAAEFVDK LVKWTKNIKI SDPFEEGCRL GPVISKGQYD KIMKFISTAK SEGATILYGG
SRPEHLKKGY YIEPTIVTDI STSMQIWKEE VFGPVLCVKT FSSEDEAIAL ANDTEYGLAA
AVFSNDLERC ERITKALEVG AVWVNCSQPC FVQAPWGGIK RSGFGRELGE WGIQNYLNIK
QVTQDISDEP WGWYKSP
