AMYS_NEIPO
ID AMYS_NEIPO Reviewed; 636 AA.
AC Q9ZEU2; Q84HD5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Amylosucrase;
DE EC=2.4.1.4 {ECO:0000269|PubMed:10767427, ECO:0000269|PubMed:10828446};
GN Name=ams;
OS Neisseria polysaccharea.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=489;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 43768 / DSM 22809 / CCUG 18030 / CIP 100113 / NCTC 11858 / LNP
RC N 462;
RX PubMed=9150231; DOI=10.1128/jb.179.10.3324-3330.1997;
RA Buettcher V., Welsh T., Willmitzer L., Kossmann J.;
RT "Cloning and characterization of the gene for amylosucrase from Neisseria
RT polysaccharea: production of a linear alpha-1,4-glucan.";
RL J. Bacteriol. 179:3324-3330(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 43768 / DSM 22809 / CCUG 18030 / CIP 100113 / NCTC 11858 / LNP
RC N 462;
RX PubMed=9882648; DOI=10.1128/jb.181.2.375-381.1999;
RA Potocki de Montalk G., Remaud-Simeon M., Willemot R.-M., Planchot V.,
RA Monsan P.;
RT "Sequence analysis of the gene encoding amylosucrase from Neisseria
RT polysaccharea and characterization of the recombinant enzyme.";
RL J. Bacteriol. 181:375-381(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=85322;
RX PubMed=12517860; DOI=10.1128/jcm.41.1.273-278.2003;
RA Zhu P., Tsang R.S.W., Tsai C.-M.;
RT "Nonencapsulated Neisseria meningitidis strain produces amylopectin from
RT sucrose: altering the concept for differentiation between N. meningitidis
RT and N. polysaccharea.";
RL J. Clin. Microbiol. 41:273-278(2003).
RN [4]
RP CHARACTERIZATION, KINETIC PARAMETERS, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43768 / DSM 22809 / CCUG 18030 / CIP 100113 / NCTC 11858 / LNP
RC N 462;
RX PubMed=10767427; DOI=10.1016/s0014-5793(00)01406-x;
RA Potocki de Montalk G., Remaud-Simeon M., Willemot R.-M., Sarcabal P.,
RA Planchot V., Monsan P.;
RT "Amylosucrase from Neisseria polysaccharea: novel catalytic properties.";
RL FEBS Lett. 471:219-223(2000).
RN [5]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-195; ASP-294; GLU-308; GLU-336;
RP GLU-352; HIS-400 AND ASP-401, AND ACTIVE SITE.
RC STRAIN=ATCC 43768 / DSM 22809 / CCUG 18030 / CIP 100113 / NCTC 11858 / LNP
RC N 462;
RX PubMed=10828446; DOI=10.1016/s0014-5793(00)01567-2;
RA Sarcabal P., Remaud-Simeon M., Willemot R.-M., Potocki de Montalk G.,
RA Svensson B., Monsan P.;
RT "Identification of key amino acid residues in Neisseria polysaccharea
RT amylosucrase.";
RL FEBS Lett. 474:33-37(2000).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 13-636 IN COMPLEX WITH D-GLUCOSE
RP AND SUCROSE.
RC STRAIN=ATCC 43768 / DSM 22809 / CCUG 18030 / CIP 100113 / NCTC 11858 / LNP
RC N 462;
RX PubMed=11467966; DOI=10.1021/bi010706l;
RA Mirza O., Skov L.K., Remaud-Simeon M., Potocki de Montalk G., Albenne C.,
RA Monsan P., Gajhede M.;
RT "Crystal structures of amylosucrase from Neisseria polysaccharea in complex
RT with D-glucose and the active site mutant Glu328Gln in complex with the
RT natural substrate sucrose.";
RL Biochemistry 40:9032-9039(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 13-636.
RC STRAIN=ATCC 43768 / DSM 22809 / CCUG 18030 / CIP 100113 / NCTC 11858 / LNP
RC N 462;
RX PubMed=11306569; DOI=10.1074/jbc.m010998200;
RA Skov L.K., Mirza O., Henriksen A., De Montalk G.P., Remaud-Simeon M.,
RA Sarcabal P., Willemot R.M., Monsan P., Gajhede M.;
RT "Amylosucrase, a glucan-synthesizing enzyme from the alpha-amylase
RT family.";
RL J. Biol. Chem. 276:25273-25278(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 13-636 OF MUTANT GLN-336 IN
RP COMPLEX WITH SUCROSE AND MALTOHEPTAOSE.
RX PubMed=12364331; DOI=10.1074/jbc.m207860200;
RA Skov L.K., Mirza O., Sprogoe D., Dar I., Remaud-Simeon M., Albenne C.,
RA Monsan P., Gajhede M.;
RT "Oligosaccharide and sucrose complexes of amylosucrase. Structural
RT implications for the polymerase activity.";
RL J. Biol. Chem. 277:47741-47747(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 13-636 OF MUTANT GLN-336 IN
RP COMPLEX WITH ALPHA-D-GLUCOPYRANOSYL FLUORIDE, AND ACTIVE SITE.
RX PubMed=15023061; DOI=10.1021/bi0357762;
RA Jensen M.H., Mirza O., Albenne C., Remaud-Simeon M., Monsan P., Gajhede M.,
RA Skov L.K.;
RT "Crystal structure of the covalent intermediate of amylosucrase from
RT Neisseria polysaccharea.";
RL Biochemistry 43:3104-3110(2004).
CC -!- FUNCTION: Catalyzes the synthesis of alpha-glucan from sucrose.
CC Catalyzes, in addition, sucrose hydrolysis, maltose and maltotriose
CC synthesis by successive transfers of the glucosyl moiety of sucrose
CC onto the released glucose, and finally turanose and trehalulose
CC synthesis, these two sucrose isomers being obtained by glucosyl
CC transfer onto fructose. {ECO:0000269|PubMed:9882648}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + sucrose = [(1->4)-alpha-D-
CC glucosyl](n+1) + D-fructose; Xref=Rhea:RHEA:24572, Rhea:RHEA-
CC COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15444, ChEBI:CHEBI:17992,
CC ChEBI:CHEBI:37721; EC=2.4.1.4; Evidence={ECO:0000269|PubMed:10767427,
CC ECO:0000269|PubMed:10828446};
CC -!- ACTIVITY REGULATION: Amylosucrase favors hydrolysis at low sucrose
CC concentrations, and polymerization at high sucrose concentrations.
CC Competitively inhibited by fructose.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for sucrose (in the sucrose consumption assay, when initial
CC sucrose < 20 mM) {ECO:0000269|PubMed:10767427};
CC KM=1.7 mM for sucrose (in the sucrose hydrolysis reaction, when
CC initial sucrose < 20 mM) {ECO:0000269|PubMed:10767427};
CC KM=1.9 mM for sucrose (in the polymerization reaction, when initial
CC sucrose < 20 mM) {ECO:0000269|PubMed:10767427};
CC KM=50.2 mM for sucrose (in the sucrose consumption assay, when
CC initial sucrose > 20 mM) {ECO:0000269|PubMed:10767427};
CC KM=38.7 mM for sucrose (in the sucrose hydrolysis reaction, when
CC initial sucrose > 20 mM) {ECO:0000269|PubMed:10767427};
CC Vmax=470 umol/min/g enzyme for sucrose consumption (when initial
CC sucrose < 20 mM) {ECO:0000269|PubMed:10767427};
CC Vmax=288 umol/min/g enzyme for sucrose hydrolysis (when initial
CC sucrose < 20 mM) {ECO:0000269|PubMed:10767427};
CC Vmax=147 umol/min/g enzyme for polymerization reaction (when initial
CC sucrose < 20 mM) {ECO:0000269|PubMed:10767427};
CC Vmax=1100 umol/min/g enzyme for sucrose consumption (when initial
CC sucrose > 20 mM) {ECO:0000269|PubMed:10767427};
CC Vmax=472 umol/min/g enzyme for sucrose hydrolysis (when initial
CC sucrose > 20 mM) {ECO:0000269|PubMed:10767427};
CC Vmax=1620 umol/min/g enzyme for polymerization reaction (when initial
CC sucrose > 20 mM) {ECO:0000269|PubMed:10767427};
CC Note=This enzyme does not present a classic Michaelis-Menten behavior
CC for sucrose consumption, that could be related to the presence of a
CC second sucrose binding site. Nevertheless, it is possible to model
CC sucrose consumption rate versus sucrose concentration by two
CC different Michaelis-Menten equations whose apparent kinetic constants
CC are given just above.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11467966,
CC ECO:0000269|PubMed:12364331, ECO:0000269|PubMed:15023061,
CC ECO:0000269|PubMed:9882648}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9150231}.
CC -!- MISCELLANEOUS: Like the recombinant protein expressed in E.coli, the
CC amylosucrase may be secreted in N.polysaccharea without cleavage of a
CC signal sequence.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ011781; CAA09772.1; -; Genomic_DNA.
DR EMBL; AY099335; AAM51153.1; -; Genomic_DNA.
DR RefSeq; WP_003751803.1; NZ_CP031325.1.
DR PDB; 1G5A; X-ray; 1.40 A; A=13-636.
DR PDB; 1JG9; X-ray; 1.66 A; A=13-636.
DR PDB; 1JGI; X-ray; 2.00 A; A=13-636.
DR PDB; 1MVY; X-ray; 2.00 A; A=13-636.
DR PDB; 1MW0; X-ray; 2.01 A; A=13-636.
DR PDB; 1MW1; X-ray; 2.10 A; A=13-636.
DR PDB; 1MW2; X-ray; 2.10 A; A=13-636.
DR PDB; 1MW3; X-ray; 2.00 A; A=13-636.
DR PDB; 1S46; X-ray; 2.20 A; A=13-636.
DR PDB; 1ZS2; X-ray; 2.16 A; A=13-636.
DR PDB; 3UEQ; X-ray; 1.85 A; A=13-636.
DR PDB; 4FLO; X-ray; 2.20 A; A=13-636.
DR PDB; 4FLQ; X-ray; 2.50 A; A=13-636.
DR PDB; 4FLR; X-ray; 2.40 A; A=13-636.
DR PDB; 4FLS; X-ray; 2.30 A; A=13-636.
DR PDB; 5N6V; X-ray; 1.60 A; A=13-636.
DR PDB; 5N7J; X-ray; 2.00 A; A=13-636.
DR PDBsum; 1G5A; -.
DR PDBsum; 1JG9; -.
DR PDBsum; 1JGI; -.
DR PDBsum; 1MVY; -.
DR PDBsum; 1MW0; -.
DR PDBsum; 1MW1; -.
DR PDBsum; 1MW2; -.
DR PDBsum; 1MW3; -.
DR PDBsum; 1S46; -.
DR PDBsum; 1ZS2; -.
DR PDBsum; 3UEQ; -.
DR PDBsum; 4FLO; -.
DR PDBsum; 4FLQ; -.
DR PDBsum; 4FLR; -.
DR PDBsum; 4FLS; -.
DR PDBsum; 5N6V; -.
DR PDBsum; 5N7J; -.
DR AlphaFoldDB; Q9ZEU2; -.
DR SMR; Q9ZEU2; -.
DR DrugBank; DB04447; 1,4-Dithiothreitol.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB02772; Sucrose.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; Q9ZEU2; -.
DR BRENDA; 2.4.1.4; 3596.
DR SABIO-RK; Q9ZEU2; -.
DR EvolutionaryTrace; Q9ZEU2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0047669; F:amylosucrase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11324; AmyAc_Amylosucrase; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR044077; Amylosucrase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase; Secreted;
KW Transferase.
FT CHAIN 1..636
FT /note="Amylosucrase"
FT /id="PRO_0000045154"
FT ACT_SITE 294
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:15023061,
FT ECO:0000305|PubMed:10828446"
FT ACT_SITE 336
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:10828446"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11467966,
FT ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11467966,
FT ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11467966,
FT ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11467966,
FT ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11467966,
FT ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"
FT BINDING 401
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11467966,
FT ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"
FT BINDING 517
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:11467966,
FT ECO:0000305|PubMed:12364331, ECO:0000305|PubMed:15023061"
FT SITE 452
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MUTAGEN 195
FT /note="H->Q: 98% reduction of activity."
FT /evidence="ECO:0000269|PubMed:10828446"
FT MUTAGEN 294
FT /note="D->E,N: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10828446"
FT MUTAGEN 308
FT /note="E->Q: No effect."
FT /evidence="ECO:0000269|PubMed:10828446"
FT MUTAGEN 336
FT /note="E->Q: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10828446"
FT MUTAGEN 352
FT /note="E->Q: 30% reduction of activity."
FT /evidence="ECO:0000269|PubMed:10828446"
FT MUTAGEN 400
FT /note="H->N: 97% reduction of activity."
FT /evidence="ECO:0000269|PubMed:10828446"
FT MUTAGEN 401
FT /note="D->E: Almost complete loss of activity."
FT /evidence="ECO:0000269|PubMed:10828446"
FT CONFLICT 14
FT /note="Y -> H (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 84..85
FT /note="NS -> SA (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="D -> N (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="A -> E (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="S -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="G -> D (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="A -> S (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="S -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="S -> N (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="A -> S (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="V -> A (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="D -> N (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="D -> S (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="L -> P (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT CONFLICT 505..510
FT /note="DWSQDS -> GWAQDG (in Ref. 3; AAM51153)"
FT /evidence="ECO:0000305"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 25..33
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 35..59
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 65..82
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 85..95
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 170..182
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 311..327
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 392..397
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 459..463
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 465..467
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 472..485
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 510..514
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 516..520
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 526..529
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 538..555
FT /evidence="ECO:0007829|PDB:1G5A"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:1JGI"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 583..588
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 598..603
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 606..610
FT /evidence="ECO:0007829|PDB:1G5A"
FT TURN 611..613
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:1G5A"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:1G5A"
SQ SEQUENCE 636 AA; 72344 MW; B7656C19BF1A2065 CRC64;
MLTPTQQVGL ILQYLKTRIL DIYTPEQRAG IEKSEDWRQF SRRMDTHFPK LMNELDSVYG
NNEALLPMLE MLLAQAWQSY SQRNSSLKDI DIARENNPDW ILSNKQVGGV CYVDLFAGDL
KGLKDKIPYF QELGLTYLHL MPLFKCPEGK SDGGYAVSSY RDVNPALGTI GDLREVIAAL
HEAGISAVVD FIFNHTSNEH EWAQRCAAGD PLFDNFYYIF PDRRMPDQYD RTLREIFPDQ
HPGGFSQLED GRWVWTTFNS FQWDLNYSNP WVFRAMAGEM LFLANLGVDI LRMDAVAFIW
KQMGTSCENL PQAHALIRAF NAVMRIAAPA VFFKSEAIVH PDQVVQYIGQ DECQIGYNPL
QMALLWNTLA TREVNLLHQA LTYRHNLPEH TAWVNYVRSH DDIGWTFADE DAAYLGISGY
DHRQFLNRFF VNRFDGSFAR GVPFQYNPST GDCRVSGTAA ALVGLAQDDP HAVDRIKLLY
SIALSTGGLP LIYLGDEVGT LNDDDWSQDS NKSDDSRWAH RPRYNEALYA QRNDPSTAAG
QIYQGLRHMI AVRQSNPRFD GGRLVTFNTN NKHIIGYIRN NALLAFGNFS EYPQTVTAHT
LQAMPFKAHD LIGGKTVSLN QDLTLQPYQV MWLEIA
