AMT4_PELSC
ID AMT4_PELSC Reviewed; 551 AA.
AC P22963;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Glucan 1,4-alpha-maltotetraohydrolase;
DE Short=G4-amylase;
DE EC=3.2.1.60;
DE AltName: Full=Exo-maltotetraohydrolase;
DE AltName: Full=Maltotetraose-forming amylase;
DE AltName: Full=Maltotetraose-forming exo-amylase;
DE Flags: Precursor;
GN Name=mta;
OS Pelomonas saccharophila (Pseudomonas saccharophila).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Pelomonas.
OX NCBI_TaxID=304;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15946 / DSM 654 / JCM 15912 / IAM 1504 / NBRC 103037 / NCIMB
RC 8570 / NRRL B-1492;
RX PubMed=2676600; DOI=10.1016/0014-5793(89)81056-7;
RA Zhou J., Baba T., Takano T., Kobayashi S., Arai Y.;
RT "Nucleotide sequence of the maltotetraohydrolase gene from Pseudomonas
RT saccharophila.";
RL FEBS Lett. 255:37-41(1989).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous
CC polysaccharides, to remove successive maltotetraose residues from the
CC non-reducing chain ends.; EC=3.2.1.60;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Glycan degradation; starch degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X16732; CAA34708.1; -; Genomic_DNA.
DR PIR; S05667; S05667.
DR PDB; 6IWK; X-ray; 1.50 A; A=22-439.
DR PDB; 6IYG; X-ray; 1.50 A; A=22-551.
DR PDB; 6J3X; X-ray; 1.62 A; A=22-551.
DR PDB; 6JQB; X-ray; 1.10 A; A=22-551.
DR PDB; 7CZJ; X-ray; 1.50 A; A/B=455-551.
DR PDBsum; 6IWK; -.
DR PDBsum; 6IYG; -.
DR PDBsum; 6J3X; -.
DR PDBsum; 6JQB; -.
DR PDBsum; 7CZJ; -.
DR AlphaFoldDB; P22963; -.
DR SMR; P22963; -.
DR CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR UniPathway; UPA00153; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0033910; F:glucan 1,4-alpha-maltotetraohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:2001070; F:starch binding; IEA:InterPro.
DR GO; GO:0005983; P:starch catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR006046; Alpha_amylase.
DR InterPro; IPR015165; AMT4_domain_C.
DR InterPro; IPR013784; Carb-bd-like_fold.
DR InterPro; IPR002044; CBM_fam20.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF00686; CBM_20; 1.
DR Pfam; PF09081; DUF1921; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SMART; SM01065; CBM_2; 1.
DR SUPFAM; SSF49452; SSF49452; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51166; CBM20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Disulfide bond;
KW Glycosidase; Hydrolase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..21
FT CHAIN 22..551
FT /note="Glucan 1,4-alpha-maltotetraohydrolase"
FT /id="PRO_0000001419"
FT DOMAIN 449..551
FT /note="CBM20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00594"
FT ACT_SITE 214
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177..181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 315
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 161..171
FT /evidence="ECO:0000250"
FT DISULFID 237..272
FT /evidence="ECO:0000250"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:6JQB"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6IWK"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 189..203
FT /evidence="ECO:0007829|PDB:6JQB"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:6JQB"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 363..376
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 389..398
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 403..409
FT /evidence="ECO:0007829|PDB:6JQB"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:6JQB"
FT TURN 430..433
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:6JQB"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:7CZJ"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:7CZJ"
FT HELIX 479..484
FT /evidence="ECO:0007829|PDB:7CZJ"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:7CZJ"
FT STRAND 494..497
FT /evidence="ECO:0007829|PDB:7CZJ"
FT STRAND 500..506
FT /evidence="ECO:0007829|PDB:7CZJ"
FT STRAND 512..524
FT /evidence="ECO:0007829|PDB:7CZJ"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:7CZJ"
FT STRAND 537..540
FT /evidence="ECO:0007829|PDB:7CZJ"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:7CZJ"
SQ SEQUENCE 551 AA; 59898 MW; F6D67D0BB235EA35 CRC64;
MSHILRAAVL AAVLLPFPAL ADQAGKSPAG VRYHGGDEII LQGFHWNVVR EAPNDWYNIL
RQQASTIAAD GFSAIWMPVP WRDFSSWTDG GKSGGGEGYF WHDFNKNGRY GSDAQLRQAA
GALGGAGVKV LYDVVPNHMN RGYPDKEINL PAGQGFWRND CADPGNYPND CDDGDRFIGG
ESDLNTGHPQ IYGMFRDELA NLRSGYGAGG FRFDFVRGYA PERVDSWMSD SADSSFCVGE
LWKGPSEYPS WDWRNTASWQ QIIKDWSDRA KCPVFDFALK ERMQNGSVAD WKHGLNGNPD
PRWREVAVTF VDNHDTGYSP GQNGGQHHWA LQDGLIRQAY AYILTSPGTP VVYWSHMYDW
GYGDFIRQLI QVRRTAGVRA DSAISFHSGY SGLVATVSGS QQTLVVALNS DLANPGQVAS
GSFSEAVNAS NGQVRVWRSG SGDGGGNDGG EGGLVNVNFR CDNGVTQMGD SVYAVGNVSQ
LGNWSPASAV RLTDTSSYPT WKGSIALPDG QNVEWKCLIR NEADATLVRQ WQSGGNNQVQ
AAAGASTSGS F
