ID SAHH_RAT Reviewed; 432 AA.
AC P10760;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 204.
DE RecName: Full=Adenosylhomocysteinase;
DE Short=AdoHcyase {ECO:0000303|PubMed:11741948, ECO:0000303|PubMed:11927587};
DE EC=3.13.2.1 {ECO:0000269|PubMed:11927587};
DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000303|PubMed:11741948};
GN Name=Ahcy;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3027698; DOI=10.1073/pnas.84.3.719;
RA Ogawa H., Gomi T., Mueckler M.M., Fujioka M., Backlund P.S. Jr.,
RA Aksamit R.R., Unson C.G., Cantoni G.L.;
RT "Amino acid sequence of S-adenosyl-L-homocysteine hydrolase from rat liver
RT as derived from the cDNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:719-723(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer 344;
RX PubMed=7744082; DOI=10.1111/j.1432-1033.1995.tb20500.x;
RA Merta A., Aksamit R.R., Kasir J., Cantoni G.L.;
RT "The gene and pseudogenes of rat S-adenosyl-L-homocysteine hydrolase.";
RL Eur. J. Biochem. 229:575-582(1995).
RN [3]
RP PROTEIN SEQUENCE OF 76-94.
RX PubMed=3759971; DOI=10.1016/s0021-9258(18)67034-6;
RA Gomi T., Ogawa H., Fujioka M.;
RT "S-adenosylhomocysteinase from rat liver. Amino acid sequences of the
RT peptides containing active site cysteine residues modified by treatment
RT with 5'-p-fluorosulfonylbenzoyladenosine.";
RL J. Biol. Chem. 261:13422-13425(1986).
RN [4]
RP PROTEIN SEQUENCE OF 143-151 AND 268-285, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NAD, COFACTOR, AND
RP SUBUNIT.
RC TISSUE=Liver;
RX PubMed=10387078; DOI=10.1021/bi990332k;
RA Hu Y., Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M.,
RA Takusagawa F.;
RT "Crystal structure of S-adenosylhomocysteine hydrolase from rat liver.";
RL Biochemistry 38:8323-8333(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT GLU-245.
RX PubMed=10913437; DOI=10.1074/jbc.m003725200;
RA Komoto J., Huang Y., Gomi T., Ogawa H., Takata Y., Fujioka M.,
RA Takusagawa F.;
RT "Effects of site-directed mutagenesis on structure and function of
RT recombinant rat liver S-adenosylhomocysteine hydrolase. Crystal structure
RT of D244E mutant enzyme.";
RL J. Biol. Chem. 275:32147-32156(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH INHIBITOR, AND
RP SUBUNIT.
RX PubMed=11741948; DOI=10.1074/jbc.m109187200;
RA Huang Y., Komoto J., Takata Y., Powell D.R., Gomi T., Ogawa H., Fujioka M.,
RA Takusagawa F.;
RT "Inhibition of S-adenosylhomocysteine hydrolase by acyclic sugar adenosine
RT analogue D-eritadenine. Crystal structure of S-adenosylhomocysteine
RT hydrolase complexed with D-eritadenine.";
RL J. Biol. Chem. 277:7477-7482(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), MUTAGENESIS OF ASP-131; LYS-186;
RP ASP-190 AND ASN-191, FUNCTION, COFACTOR, PATHWAY, AND CATALYTIC ACTIVITY.
RX PubMed=11927587; DOI=10.1074/jbc.m201116200;
RA Takata Y., Yamada T., Huang Y., Komoto J., Gomi T., Ogawa H., Fujioka M.,
RA Takusagawa F.;
RT "Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed
RT mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190.";
RL J. Biol. Chem. 277:22670-22676(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of S-adenosyl-L-homocysteine to form
CC adenosine and homocysteine (PubMed:11927587). Binds copper ions (By
CC similarity). {ECO:0000250|UniProtKB:P50247,
CC ECO:0000269|PubMed:11927587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenosine + L-homocysteine;
CC Xref=Rhea:RHEA:21708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16335,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58199; EC=3.13.2.1;
CC Evidence={ECO:0000269|PubMed:11927587};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21709;
CC Evidence={ECO:0000269|PubMed:11927587};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:10387078, ECO:0000269|PubMed:10913437,
CC ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
CC ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
CC ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5, ECO:0007744|PDB:1XWF,
CC ECO:0007744|PDB:2H5L};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:10387078,
CC ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
CC ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
CC ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1KY4,
CC ECO:0007744|PDB:1KY5, ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L};
CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC {ECO:0000305|PubMed:11927587}.
CC -!- SUBUNIT: Homotetramer. Interaction with AHCYL1 (By similarity).
CC {ECO:0000250|UniProtKB:P23526, ECO:0000269|PubMed:10387078,
CC ECO:0000269|PubMed:11741948}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23526}.
CC Melanosome {ECO:0000250|UniProtKB:P23526}. Nucleus
CC {ECO:0000250|UniProtKB:P23526}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P23526}.
CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC {ECO:0000305}.
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DR EMBL; M15185; AAA40705.1; -; mRNA.
DR EMBL; U14937; AAA92043.1; -; Genomic_DNA.
DR PIR; A26583; A26583.
DR RefSeq; NP_058897.1; NM_017201.1.
DR PDB; 1B3R; X-ray; 2.80 A; A/B/C/D=2-432.
DR PDB; 1D4F; X-ray; 2.80 A; A/B/C/D=2-432.
DR PDB; 1K0U; X-ray; 3.00 A; A/B/C/D/E/F/G/H=2-432.
DR PDB; 1KY4; X-ray; 2.80 A; A/B/C/D=2-432.
DR PDB; 1KY5; X-ray; 2.80 A; A/B/C/D=2-432.
DR PDB; 1XWF; X-ray; 2.80 A; A/B/C/D=2-432.
DR PDB; 2H5L; X-ray; 2.80 A; A/B/C/D/E/F/G/H=2-432.
DR PDBsum; 1B3R; -.
DR PDBsum; 1D4F; -.
DR PDBsum; 1K0U; -.
DR PDBsum; 1KY4; -.
DR PDBsum; 1KY5; -.
DR PDBsum; 1XWF; -.
DR PDBsum; 2H5L; -.
DR AlphaFoldDB; P10760; -.
DR SMR; P10760; -.
DR BioGRID; 248089; 1.
DR IntAct; P10760; 1.
DR STRING; 10116.ENSRNOP00000024310; -.
DR BindingDB; P10760; -.
DR ChEMBL; CHEMBL3118; -.
DR iPTMnet; P10760; -.
DR PhosphoSitePlus; P10760; -.
DR World-2DPAGE; 0004:P10760; -.
DR jPOST; P10760; -.
DR PaxDb; 10116-ENSRNOP00000024310; -.
DR Ensembl; ENSRNOT00000024310.4; ENSRNOP00000024310.1; ENSRNOG00000017777.4.
DR Ensembl; ENSRNOT00055008970; ENSRNOP00055006834; ENSRNOG00055005580.
DR Ensembl; ENSRNOT00055041423; ENSRNOP00055033707; ENSRNOG00055024122.
DR Ensembl; ENSRNOT00060013030; ENSRNOP00060009886; ENSRNOG00060007906.
DR Ensembl; ENSRNOT00060046660; ENSRNOP00060038798; ENSRNOG00060026924.
DR Ensembl; ENSRNOT00065017660; ENSRNOP00065013557; ENSRNOG00065010890.
DR Ensembl; ENSRNOT00065048058; ENSRNOP00065039458; ENSRNOG00065027869.
DR GeneID; 29443; -.
DR KEGG; rno:29443; -.
DR UCSC; RGD:69260; rat.
DR AGR; RGD:69260; -.
DR CTD; 191; -.
DR RGD; 69260; Ahcy.
DR eggNOG; KOG1370; Eukaryota.
DR GeneTree; ENSGT00950000182981; -.
DR HOGENOM; CLU_025194_2_1_1; -.
DR InParanoid; P10760; -.
DR OMA; YIGVTVE; -.
DR OrthoDB; 120477at2759; -.
DR PhylomeDB; P10760; -.
DR TreeFam; TF300415; -.
DR BioCyc; MetaCyc:MONOMER-8582; -.
DR BRENDA; 3.3.1.1; 5301.
DR Reactome; R-RNO-156581; Methylation.
DR Reactome; R-RNO-1614635; Sulfur amino acid metabolism.
DR SABIO-RK; P10760; -.
DR UniPathway; UPA00314; UER00076.
DR EvolutionaryTrace; P10760; -.
DR PRO; PR:P10760; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000017777; Expressed in liver and 19 other cell types or tissues.
DR Genevisible; P10760; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004013; F:adenosylhomocysteinase activity; IDA:UniProtKB.
DR GO; GO:0098604; F:adenosylselenohomocysteinase activity; TAS:Reactome.
DR GO; GO:0030554; F:adenyl nucleotide binding; IDA:RGD.
DR GO; GO:0005507; F:copper ion binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0051287; F:NAD binding; IDA:RGD.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; IMP:RGD.
DR GO; GO:0042745; P:circadian sleep/wake cycle; IDA:RGD.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IDA:RGD.
DR GO; GO:0019510; P:S-adenosylhomocysteine catabolic process; IDA:RGD.
DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central.
DR CDD; cd00401; SAHH; 1.
DR Gene3D; 3.40.50.1480; Adenosylhomocysteinase-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00563; AdoHcyase; 1.
DR InterPro; IPR042172; Adenosylhomocyst_ase-like_sf.
DR InterPro; IPR000043; Adenosylhomocysteinase-like.
DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR NCBIfam; TIGR00936; ahcY; 1.
DR PANTHER; PTHR23420; ADENOSYLHOMOCYSTEINASE; 1.
DR PANTHER; PTHR23420:SF0; ADENOSYLHOMOCYSTEINASE; 1.
DR Pfam; PF05221; AdoHcyase; 2.
DR Pfam; PF00670; AdoHcyase_NAD; 1.
DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR SMART; SM00996; AdoHcyase; 1.
DR SMART; SM00997; AdoHcyase_NAD; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00738; ADOHCYASE_1; 1.
DR PROSITE; PS00739; ADOHCYASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Cytoplasm; Direct protein sequencing;
KW Endoplasmic reticulum; Hydrolase; Hydroxylation; NAD; Nucleus;
KW One-carbon metabolism; Phosphoprotein; Reference proteome.
FT CHAIN 1..432
FT /note="Adenosylhomocysteinase"
FT /id="PRO_0000116905"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11741948"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11927587"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11741948"
FT BINDING 157..159
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10913437,
FT ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
FT ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT ECO:0007744|PDB:1KY5, ECO:0007744|PDB:2H5L"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11741948,
FT ECO:0000269|PubMed:11927587"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11741948,
FT ECO:0000269|PubMed:11927587"
FT BINDING 222..227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078"
FT BINDING 248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10913437,
FT ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
FT ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1XWF,
FT ECO:0007744|PDB:2H5L"
FT BINDING 299..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078,
FT ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
FT ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078,
FT ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
FT ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT BINDING 353
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078,
FT ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1D4F,
FT ECO:0007744|PDB:1K0U, ECO:0007744|PDB:1XWF,
FT ECO:0007744|PDB:2H5L"
FT BINDING 426..430
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078"
FT BINDING 426
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078,
FT ECO:0000269|PubMed:11741948, ECO:0000269|PubMed:11927587,
FT ECO:0007744|PDB:1B3R, ECO:0007744|PDB:1K0U,
FT ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT BINDING 430
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:10387078,
FT ECO:0000269|PubMed:10913437, ECO:0000269|PubMed:11741948,
FT ECO:0000269|PubMed:11927587, ECO:0007744|PDB:1B3R,
FT ECO:0007744|PDB:1D4F, ECO:0007744|PDB:1K0U,
FT ECO:0007744|PDB:1KY4, ECO:0007744|PDB:1KY5,
FT ECO:0007744|PDB:1XWF, ECO:0007744|PDB:2H5L"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT MOD_RES 186
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23526"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P50247"
FT MUTAGEN 131
FT /note="D->N: Strongly reduces S-adenosyl-L-homocysteine
FT hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11927587"
FT MUTAGEN 186
FT /note="K->N: Strongly reduces S-adenosyl-L-homocysteine
FT hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11927587"
FT MUTAGEN 190
FT /note="D->N: Strongly reduces S-adenosyl-L-homocysteine
FT hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11927587"
FT MUTAGEN 191
FT /note="N->S: Strongly reduces S-adenosyl-L-homocysteine
FT hydrolase activity."
FT /evidence="ECO:0000269|PubMed:11927587"
FT MUTAGEN 245
FT /note="D->E: Changes active site geometry and alters
FT affinity for NAD."
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1D4F"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1XWF"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 192..207
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 223..234
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 355..374
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 388..398
FT /evidence="ECO:0007829|PDB:1B3R"
FT TURN 399..402
FT /evidence="ECO:0007829|PDB:1B3R"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:1B3R"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:1B3R"
SQ SEQUENCE 432 AA; 47538 MW; 93CA5BED07B4FCDE CRC64;
MADKLPYKVA DIGLAAWGRK ALDIAENEMP GLMRMREMYS ASKPLKGARI AGCLHMTVET
AVLIETLVAL GAEVRWSSCN IFSTQDHAAA AIAKAGIPVF AWKGETDEEY LWCIEQTLHF
KDGPLNMILD DGGDLTNLIH TKHPQLLSGI RGISEETTTG VHNLYKMMAN GILKVPAINV
NDSVTKSKFD NLYGCRESLI DGIKRATDVM IAGKVAVVAG YGDVGKGCAQ ALRGFGARVI
ITEIDPINAL QAAMEGYEVT TMDEACKEGN IFVTTTGCVD IILGRHFEQM KDDAIVCNIG
HFDVEIDVKW LNENAVEKVN IKPQVDRYLL KNGHRIILLA EGRLVNLGCA MGHPSFVMSN
SFTNQVMAQI ELWTHPDKYP VGVHFLPKKL DEAVAEAHLG KLNVKLTKLT EKQAQYLGMP
INGPFKPDHY RY
//
