AGAL_THEMA
ID AGAL_THEMA Reviewed; 552 AA.
AC G4FEF4; O33835;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Alpha-galactosidase {ECO:0000303|PubMed:9741105, ECO:0000312|EMBL:AGL50123.1, ECO:0000312|EMBL:CAA04514.1};
DE EC=3.2.1.22 {ECO:0000269|PubMed:17323919, ECO:0000269|PubMed:24237145, ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:26005928, ECO:0000269|PubMed:27783466, ECO:0000269|PubMed:9741105};
DE AltName: Full=Melibiase {ECO:0000305};
GN Name=galA {ECO:0000303|PubMed:9741105, ECO:0000312|EMBL:CAA04514.1};
GN OrderedLocusNames=TM_1192 {ECO:0000312|EMBL:AAD36267.1};
GN ORFNames=Tmari_1199 {ECO:0000312|EMBL:AGL50123.1};
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274 {ECO:0000312|EMBL:AGL50123.1};
RN [1] {ECO:0000312|EMBL:CAA04514.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-36, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP SUBUNIT, AND OPERON STRUCTURE.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000312|EMBL:CAA04514.1};
RX PubMed=9741105; DOI=10.1016/s0723-2020(98)80002-7;
RA Liebl W., Wagner B., Schellhase J.;
RT "Properties of an alpha-galactosidase, and structure of its gene galA,
RT within an alpha- and beta-galactoside utilization gene cluster of the
RT hyperthermophilic bacterium Thermotoga maritima.";
RL Syst. Appl. Microbiol. 21:1-11(1998).
RN [2] {ECO:0000312|EMBL:AAD36267.1, ECO:0000312|Proteomes:UP000008183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000312|EMBL:AAD36267.1, ECO:0000312|Proteomes:UP000008183};
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3] {ECO:0000312|EMBL:AGL50123.1, ECO:0000312|Proteomes:UP000013901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000312|EMBL:AGL50123.1, ECO:0000312|Proteomes:UP000013901};
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [4]
RP CATALYTIC ACTIVITY, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF
RP ASP-220; ASP-327 AND ASP-387.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000303|PubMed:17323919};
RX PubMed=17323919; DOI=10.1021/bi061521n;
RA Comfort D.A., Bobrov K.S., Ivanen D.R., Shabalin K.A., Harris J.M.,
RA Kulminskaya A.A., Brumer H., Kelly R.M.;
RT "Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase
RT (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside
RT hydrolases.";
RL Biochemistry 46:3319-3330(2007).
RN [5]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-328;
RP GLY-385 AND PRO-402, AND PROTEIN ENGINEERING.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000303|PubMed:24237145};
RX PubMed=24237145; DOI=10.1134/s0006297913100052;
RA Bobrov K.S., Borisova A.S., Eneyskaya E.V., Ivanen D.R., Shabalin K.A.,
RA Kulminskaya A.A., Rychkov G.N.;
RT "Improvement of the efficiency of transglycosylation catalyzed by alpha-
RT galactosidase from Thermotoga maritima by protein engineering.";
RL Biochemistry (Mosc.) 78:1112-1123(2013).
RN [6]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000303|PubMed:26005928};
RX PubMed=26005928; DOI=10.1016/j.carres.2015.03.021;
RA Borisova A.S., Reddy S.K., Ivanen D.R., Bobrov K.S., Eneyskaya E.V.,
RA Rychkov G.N., Sandgren M., Staalbrand H., Sinnott M.L., Kulminskaya A.A.,
RA Shabalin K.A.;
RT "The method of integrated kinetics and its applicability to the exo-
RT glycosidase-catalyzed hydrolysis of p-nitrophenyl glycosides.";
RL Carbohydr. Res. 412:43-49(2015).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8
RC {ECO:0000303|PubMed:25486100};
RX PubMed=25486100; DOI=10.1016/j.carres.2014.11.003;
RA Borisova A.S., Ivanen D.R., Bobrov K.S., Eneyskaya E.V., Rychkov G.N.,
RA Sandgren M., Kulminskaya A.A., Sinnott M.L., Shabalin K.A.;
RT "alpha-Galactobiosyl units: thermodynamics and kinetics of their formation
RT by transglycosylations catalysed by the GH36 alpha-galactosidase from
RT Thermotoga maritima.";
RL Carbohydr. Res. 401:115-121(2015).
RN [8] {ECO:0007744|PDB:1ZY9}
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) OF APOENZYME.
RG Joint Center for Structural Genomics (JCSG);
RT "Crystal structure of alpha-galactosidase (ec 3.2.1.22) (melibiase)
RT (tm1192) from Thermotoga maritima at 2.34 A resolution.";
RL Submitted (JUN-2005) to the PDB data bank.
RN [9] {ECO:0007744|PDB:5M0X, ECO:0007744|PDB:5M12, ECO:0007744|PDB:5M16, ECO:0007744|PDB:5M1I}
RP X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF SUBSTRATE-FREE ENZYME AND IN
RP COMPLEX WITH INHIBITOR ANALOG AND HYDROLYSIS PRODUCT, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND REACTION MECHANISM.
RX PubMed=27783466; DOI=10.1002/anie.201607431;
RA Adamson C., Pengelly R.J., Shamsi Kazem Abadi S., Chakladar S., Draper J.,
RA Britton R., Gloster T.M., Bennet A.J.;
RT "Structural snapshots for mechanism-based inactivation of a glycoside
RT hydrolase by cyclopropyl carbasugars.";
RL Angew. Chem. Int. Ed. 55:14978-14982(2016).
CC -!- FUNCTION: Hydrolyzes the short-chain alpha-galactosaccharides
CC raffinose, melibiose and stachyose. {ECO:0000269|PubMed:25486100,
CC ECO:0000269|PubMed:9741105}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000269|PubMed:17323919, ECO:0000269|PubMed:24237145,
CC ECO:0000269|PubMed:25486100, ECO:0000269|PubMed:26005928,
CC ECO:0000269|PubMed:27783466, ECO:0000269|PubMed:9741105};
CC -!- ACTIVITY REGULATION: Inhibited by hydrolyzation product alpha-
CC galactopyranose and to a lesser extent by beta-galactopyranose, its
CC mutarotational product (PubMed:26005928). Inhibited by synthetic
CC cyclopropyl carbasugars (PubMed:27783466).
CC {ECO:0000269|PubMed:26005928, ECO:0000269|PubMed:27783466}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.075 mM for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75
CC degrees Celsius) {ECO:0000269|PubMed:9741105};
CC KM=2.100 mM for raffinose (at pH 5.0 and 75 degrees Celsius)
CC {ECO:0000269|PubMed:9741105};
CC KM=0.110 mM for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0
CC and 37 degrees Celsius) {ECO:0000269|PubMed:24237145};
CC KM=1.170 mM for melibiose (at pH 5.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:25486100};
CC KM=10.040 mM for raffinose (at pH 5.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:25486100};
CC KM=2.840 mM for stachyose (at pH 5.0 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:25486100};
CC Vmax=166 umol/min/mg enzyme for 4-nitrophenol-alpha-galactoside (at
CC pH 5.0 and 75 degrees Celsius) {ECO:0000269|PubMed:9741105};
CC Vmax=103 umol/min/mg enzyme for raffinose (at pH 5.0 and 75 degrees
CC Celsius) {ECO:0000269|PubMed:9741105};
CC Note=kcat is 176 s(1) for p-nitrophenol-alpha-galactoside (at pH 5.0
CC and 75 degrees Celsius). kcat is 109 s(1) for raffinose (at pH 5.0
CC and 75 degrees Celsius) (PubMed:9741105). kcat is 8 s(1) for p-
CC nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37 degrees
CC Celsius) (PubMed:24237145). kcat is 2.33 s(1) for melibiose (at pH
CC 5.0 and 37 degrees Celsius). kcat is 5.0 s(1) for raffinose (at pH
CC 5.0 and 37 degrees Celsius). kcat is 0.53 s(1) for stachyose (at pH
CC 5.0 and 37 degrees Celsius) (PubMed:25486100).
CC {ECO:0000269|PubMed:24237145, ECO:0000269|PubMed:25486100,
CC ECO:0000269|PubMed:9741105};
CC pH dependence:
CC Optimum pH is 5.0-5.5 when using synthetic substrate p-nitrophenyl-
CC alpha-D-galactopyranoside. {ECO:0000269|PubMed:9741105};
CC Temperature dependence:
CC Optimum temperature is 90-95 degrees Celsius when using synthetic
CC substrate p-nitrophenyl-alpha-D-galactopyranoside. The half-life of
CC thermoinactivation is 6.5 h at 85 degrees Celsius.
CC {ECO:0000269|PubMed:9741105};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9741105}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 36 family. {ECO:0000305}.
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DR EMBL; AJ001072; CAA04514.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36267.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL50123.1; -; Genomic_DNA.
DR PIR; E72283; E72283.
DR RefSeq; NP_228997.1; NC_000853.1.
DR RefSeq; WP_004080136.1; NZ_CP011107.1.
DR PDB; 1ZY9; X-ray; 2.34 A; A=1-552.
DR PDB; 5M0X; X-ray; 1.80 A; A=1-552.
DR PDB; 5M12; X-ray; 1.53 A; A=1-552.
DR PDB; 5M16; X-ray; 1.62 A; A=1-552.
DR PDB; 5M1I; X-ray; 1.55 A; A=1-552.
DR PDB; 6GTA; X-ray; 2.20 A; A=1-552.
DR PDB; 6GVD; X-ray; 1.22 A; A=1-552.
DR PDB; 6GWF; X-ray; 1.72 A; A=1-552.
DR PDB; 6GWG; X-ray; 1.77 A; A=1-552.
DR PDB; 6GX8; X-ray; 1.42 A; A=1-552.
DR PDBsum; 1ZY9; -.
DR PDBsum; 5M0X; -.
DR PDBsum; 5M12; -.
DR PDBsum; 5M16; -.
DR PDBsum; 5M1I; -.
DR PDBsum; 6GTA; -.
DR PDBsum; 6GVD; -.
DR PDBsum; 6GWF; -.
DR PDBsum; 6GWG; -.
DR PDBsum; 6GX8; -.
DR AlphaFoldDB; G4FEF4; -.
DR SMR; G4FEF4; -.
DR STRING; 243274.THEMA_08370; -.
DR ChEMBL; CHEMBL3308963; -.
DR CAZy; GH36; Glycoside Hydrolase Family 36.
DR DNASU; 898292; -.
DR EnsemblBacteria; AAD36267; AAD36267; TM_1192.
DR EnsemblBacteria; AGL50123; AGL50123; Tmari_1199.
DR KEGG; tma:TM1192; -.
DR KEGG; tmm:Tmari_1199; -.
DR KEGG; tmw:THMA_1218; -.
DR PATRIC; fig|243274.17.peg.1197; -.
DR eggNOG; COG3345; Bacteria.
DR InParanoid; G4FEF4; -.
DR OMA; ILGCGAP; -.
DR OrthoDB; 469334at2; -.
DR BRENDA; 3.2.1.22; 6331.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016139; P:glycoside catabolic process; IDA:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..552
FT /note="Alpha-galactosidase"
FT /id="PRO_0000439021"
FT ACT_SITE 327
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:17323919"
FT ACT_SITE 387
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:17323919"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27783466,
FT ECO:0007744|PDB:5M16"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27783466,
FT ECO:0007744|PDB:5M16"
FT BINDING 220..221
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27783466,
FT ECO:0007744|PDB:5M16"
FT BINDING 325..327
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27783466,
FT ECO:0007744|PDB:5M16"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27783466,
FT ECO:0007744|PDB:5M16"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27783466,
FT ECO:0007744|PDB:5M16"
FT MUTAGEN 220
FT /note="D->A: Less than 1% of the wild-type enzyme activity
FT with p-nitrophenyl-alpha-D-galactopyranoside as substrate
FT at 80 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:17323919"
FT MUTAGEN 220
FT /note="D->G: Reduced activity compared to the wild-type
FT enzyme."
FT /evidence="ECO:0000269|PubMed:17323919"
FT MUTAGEN 327
FT /note="D->A: Less than 1% of the wild-type enzyme activity
FT with p-nitrophenyl-alpha-D-galactopyranoside as substrate
FT at 80 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:17323919"
FT MUTAGEN 327
FT /note="D->G: Between 200 and 800-fold lower catalytic rate
FT and between 300 and 1700-fold lower catalytic efficiency
FT than the wild-type enzyme with aryl-alpha-galactosides as
FT substrates."
FT /evidence="ECO:0000269|PubMed:17323919"
FT MUTAGEN 328
FT /note="F->A: Increased transglycosylating activity at high
FT concentrations of p-nitrophenyl-alpha-D-galactopyranoside
FT substrate, which could be useful in industry and medicine
FT for the synthesis of different p-nitrophenyl-
FT digalactosides. Able to produce 16 times more of a regio-
FT isomer with the (alpha1,2)-bond than wild-type enzyme."
FT /evidence="ECO:0000269|PubMed:24237145"
FT MUTAGEN 385
FT /note="G->L: Increased transglycosylating activity at high
FT concentrations of p-nitrophenyl-alpha-D-galactopyranoside
FT substrate, which could be useful in industry and medicine
FT for the synthesis of different p-nitrophenyl-
FT digalactosides."
FT /evidence="ECO:0000269|PubMed:24237145"
FT MUTAGEN 387
FT /note="D->A: Less than 1% of the wild-type enzyme activity
FT with p-nitrophenyl-alpha-D-galactopyranoside as substrate
FT at 80 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:17323919"
FT MUTAGEN 387
FT /note="D->G: 1500-fold lower catalytic rate and 1000-fold
FT lower catalytic efficiency than the wild-type enzyme with
FT p-nitrophenyl-alpha-D-galactopyranoside as substrate."
FT /evidence="ECO:0000269|PubMed:17323919"
FT MUTAGEN 402
FT /note="P->D: Increased transglycosylating activity at high
FT concentrations of p-nitrophenyl-alpha-D-galactopyranoside
FT substrate, which could be useful in industry and medicine
FT for the synthesis of different p-nitrophenyl-
FT digalactosides."
FT /evidence="ECO:0000269|PubMed:24237145"
FT STRAND 1..3
FT /evidence="ECO:0007829|PDB:1ZY9"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 18..29
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 32..41
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1ZY9"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 160..175
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 199..208
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 303..319
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:6GVD"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 404..413
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:6GVD"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 421..425
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 440..452
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6GVD"
FT HELIX 468..478
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 482..487
FT /evidence="ECO:0007829|PDB:6GVD"
FT TURN 488..491
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 493..504
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:6GVD"
FT TURN 515..518
FT /evidence="ECO:0007829|PDB:6GVD"
FT STRAND 519..524
FT /evidence="ECO:0007829|PDB:6GVD"
SQ SEQUENCE 552 AA; 63657 MW; 91C6E6EFA24EA9D5 CRC64;
MEIFGKTFRE GRFVLKEKNF TVEFAVEKIH LGWKISGRVK GSPGRLEVLR TKAPEKVLVN
NWQSWGPCRV VDAFSFKPPE IDPNWRYTAS VVPDVLERNL QSDYFVAEEG KVYGFLSSKI
AHPFFAVEDG ELVAYLEYFD VEFDDFVPLE PLVVLEDPNT PLLLEKYAEL VGMENNARVP
KHTPTGWCSW YHYFLDLTWE ETLKNLKLAK NFPFEVFQID DAYEKDIGDW LVTRGDFPSV
EEMAKVIAEN GFIPGIWTAP FSVSETSDVF NEHPDWVVKE NGEPKMAYRN WNKKIYALDL
SKDEVLNWLF DLFSSLRKMG YRYFKIDFLF AGAVPGERKK NITPIQAFRK GIETIRKAVG
EDSFILGCGS PLLPAVGCVD GMRIGPDTAP FWGEHIEDNG APAARWALRN AITRYFMHDR
FWLNDPDCLI LREEKTDLTQ KEKELYSYTC GVLDNMIIES DDLSLVRDHG KKVLKETLEL
LGGRPRVQNI MSEDLRYEIV SSGTLSGNVK IVVDLNSREY HLEKEGKSSL KKRVVKREDG
RNFYFYEEGE RE
