AMT6_BACS7
ID AMT6_BACS7 Reviewed; 518 AA.
AC P19571;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glucan 1,4-alpha-maltohexaosidase;
DE EC=3.2.1.98 {ECO:0000250|UniProtKB:P06278};
DE AltName: Full=Exo-maltohexaohydrolase;
DE AltName: Full=G6-amylase;
DE AltName: Full=Maltohexaose-producing amylase;
DE Flags: Precursor;
OS Bacillus sp. (strain 707).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1416;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 34-36.
RX PubMed=3258152; DOI=10.1016/0006-291x(88)90554-2;
RA Tsukamoto A., Kimura K., Ishii Y., Takano T., Yamane K.;
RT "Nucleotide sequence of the maltohexaose-producing amylase gene from an
RT alkalophilic Bacillus sp. #707 and structural similarity to liquefying type
RT alpha-amylases.";
RL Biochem. Biophys. Res. Commun. 151:25-31(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous
CC polysaccharides, to remove successive maltohexaose residues from the
CC non-reducing chain ends.; EC=3.2.1.98;
CC Evidence={ECO:0000250|UniProtKB:P06278};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P06278};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P06278};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000250|UniProtKB:P06278};
CC Note=Binds 1 sodium ion per subunit. {ECO:0000250|UniProtKB:P06278};
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; M18862; AAA22231.1; -; Genomic_DNA.
DR PIR; A27705; A27705.
DR PDB; 1WP6; X-ray; 2.10 A; A=34-518.
DR PDB; 1WPC; X-ray; 1.90 A; A=34-518.
DR PDB; 2D3L; X-ray; 2.30 A; A=34-518.
DR PDB; 2D3N; X-ray; 1.90 A; A=34-518.
DR PDB; 2GJP; X-ray; 1.90 A; A=34-516.
DR PDB; 2GJR; X-ray; 2.10 A; A=34-516.
DR PDBsum; 1WP6; -.
DR PDBsum; 1WPC; -.
DR PDBsum; 2D3L; -.
DR PDBsum; 2D3N; -.
DR PDBsum; 2GJP; -.
DR PDBsum; 2GJR; -.
DR AlphaFoldDB; P19571; -.
DR SMR; P19571; -.
DR DrugBank; DB01841; 4,6-Dideoxyglucose.
DR DrugBank; DB02120; 6-Amino-4-Hydroxymethyl-Cyclohex-4-Ene-1,2,3-Triol.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR BRENDA; 3.2.1.98; 691.
DR UniPathway; UPA00153; -.
DR EvolutionaryTrace; P19571; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0033927; F:glucan 1,4-alpha-maltohexaosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR013776; A-amylase_thermo.
DR InterPro; IPR015237; Alpha-amylase_C_pro.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09154; DUF1939; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:3258152"
FT CHAIN 34..518
FT /note="Glucan 1,4-alpha-maltohexaosidase"
FT /id="PRO_0000001421"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 299
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 196
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 196
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 221
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 232
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 238
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P00692"
FT SITE 366
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 56..70
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:1WPC"
FT TURN 179..183
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1WPC"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2GJP"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 244..261
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 264..268
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:1WPC"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 324..334
FT /evidence="ECO:0007829|PDB:1WPC"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:1WPC"
FT TURN 345..348
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1WPC"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 368..371
FT /evidence="ECO:0007829|PDB:1WP6"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 391..400
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 401..405
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 416..428
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 459..467
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:1WPC"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:1WPC"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:1WPC"
SQ SEQUENCE 518 AA; 59009 MW; 3A961E21612682C4 CRC64;
MKMRTGKKGF LSILLAFLLV ITSIPFTLVD VEAHHNGTNG TMMQYFEWYL PNDGNHWNRL
NSDASNLKSK GITAVWIPPA WKGASQNDVG YGAYDLYDLG EFNQKGTVRT KYGTRSQLQA
AVTSLKNNGI QVYGDVVMNH KGGADATEMV RAVEVNPNNR NQEVTGEYTI EAWTRFDFPG
RGNTHSSFKW RWYHFDGVDW DQSRRLNNRI YKFRGHGKAW DWEVDTENGN YDYLMYADID
MDHPEVVNEL RNWGVWYTNT LGLDGFRIDA VKHIKYSFTR DWINHVRSAT GKNMFAVAEF
WKNDLGAIEN YLQKTNWNHS VFDVPLHYNL YNASKSGGNY DMRNIFNGTV VQRHPSHAVT
FVDNHDSQPE EALESFVEEW FKPLAYALTL TREQGYPSVF YGDYYGIPTH GVPAMRSKID
PILEARQKYA YGKQNDYLDH HNIIGWTREG NTAHPNSGLA TIMSDGAGGS KWMFVGRNKA
GQVWSDITGN RTGTVTINAD GWGNFSVNGG SVSIWVNK
