ID   ISOA_PSEUM              Reviewed;         776 AA.
AC   P26501;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Isoamylase;
DE            EC=3.2.1.68;
DE   Flags: Precursor;
GN   Name=iam;
OS   Pseudomonas sp. (strain SMP1).
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=72588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 27-44.
RX   PubMed=2778432; DOI=10.1099/00221287-135-1-37;
RA   Tognoni A., Carrera P., Galli G., Lucchese G., Camerini B., Grandi G.;
RT   "Cloning and nucleotide sequence of the isoamylase gene from a strain of
RT   Pseudomonas sp.";
RL   J. Gen. Microbiol. 135:37-45(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC         glycogen, amylopectin and their beta-limit dextrins.; EC=3.2.1.68;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- INDUCTION: By maltose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; M25247; AAA25855.1; -; Genomic_DNA.
DR   AlphaFoldDB; P26501; -.
DR   SMR; P26501; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0004133; F:glycogen debranching enzyme activity; IEA:UniProt.
DR   GO; GO:0019156; F:isoamylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR044505; GlgX_Isoamylase_N_E_set.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Metal-binding; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:2778432"
FT   CHAIN           27..776
FT                   /note="Isoamylase"
FT                   /id="PRO_0000001425"
FT   ACT_SITE        401
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        461
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            536
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   DISULFID        410..422
FT                   /evidence="ECO:0000250"
FT   DISULFID        546..616
FT                   /evidence="ECO:0000250"
FT   DISULFID        738..766
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   776 AA;  83657 MW;  A5E4C02EF026A3A4 CRC64;
     MKCPKILAAL LGCAVLAGVP AMPAHAAINS MSLGASYDAQ QANITFRVYS SQATRIVLYL
     YSAGYGVQES ATYTLSPAGS GVWAVTVPVS SIKAAGITGA VYYGYRAWGP NWPYASNWGK
     GSQAGFVSDV DANGDRFNPN KLLLDPYAQE VSQDPLNPSN QNGNVFASGA SYRTTDSGIY
     APKGVVLVPS TQSTGTKPTR AQKDDVIYEV HVRGFTEQDT SIPAQYRGTY YGAGLKASYL
     ASLGVTAVEF LPVQETQNDA NDVVPNSDAN QNYWGYMTEN YFSPDRRYAY NKAAGGPTAE
     FQAMVQAFHN AGIKVYMDVV YNHTAEGGTW TSSDPTTATI YSWRGLDNTT YYELTSGNQY
     FYDNTGIGAN FNTYNTVAQN LIVDSLAYWA NTMGVDGFRF DLASVLGNSC LNGAYTASAP
     NCPNGGYNFD AADSNVAINR ILREFTVRPA AGGSGLDLFA EPWAIGGNSY QLGGFPQGWS
     EWNGLFRDSL RQAQNELGSM TIYVTQDAND FSGSSNLFQS SGRSPWNSIN FIDVHDGMTL
     KDVYSCNGAN NSQAWPYGPS DGGTSTNYSW DQGMSAGTGA AVDQRRAART GMAFEMLSAG
     TPLMQGGDEY LRTLQCNNNA YNLDSSANWL TYSWTTDQSN FYTFAQRLIA FRKAHPALRP
     SSWYSGSQLT WYQPSGAVAD SNYWNNTSNY AIAYAINGPS LGDSNSIYVA YNGWSSSVTF
     TLPAPPSGTQ WYRVTDTCDW NDGASTFVAP GSETLIGGAG TTYGQCGQSL LLLISK