ID   IMD_ARTGO               Reviewed;         641 AA.
AC   Q44052;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Isomalto-dextranase;
DE            EC=3.2.1.94;
DE   AltName: Full=Exo-isomaltohydrolase;
DE   AltName: Full=Glucan 1,6-alpha-isomaltosidase;
DE   Flags: Precursor;
GN   Name=imd;
OS   Arthrobacter globiformis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=T6;
RX   PubMed=8002600; DOI=10.1128/jb.176.24.7730-7734.1994;
RA   Iwai A., Ito H., Mizuno T., Mori H., Matsui H., Honma M., Okada G.,
RA   Chiba S.;
RT   "Molecular cloning and expression of an isomalto-dextranase gene from
RT   Arthrobacter globiformis T6.";
RL   J. Bacteriol. 176:7730-7734(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in
CC         polysaccharides, to remove successive isomaltose units from the non-
CC         reducing ends of the chains.; EC=3.2.1.94;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; D30761; BAA06424.1; -; Genomic_DNA.
DR   PIR; A55549; A55549.
DR   AlphaFoldDB; Q44052; -.
DR   SMR; Q44052; -.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0015925; F:galactosidase activity; IEA:UniProt.
DR   GO; GO:0033923; F:glucan 1,6-alpha-isomaltosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR041233; Melibiase_C.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..39
FT                   /note="Tat-type signal"
FT   CHAIN           40..641
FT                   /note="Isomalto-dextranase"
FT                   /id="PRO_0000001022"
FT   DOMAIN          500..640
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   REGION          556..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        288
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   641 AA;  69765 MW;  B7F8F278F4D88350 CRC64;
     MMNLSRRTLL TTGSAATLAY ALGMAGSAQA ATAVTARPGV PVTAAPPLRL ASRNSVFTRS
     GAGPRYWNIY GYSFPHNAPI PENEWKANID WLAGNFADFG YDIACTDGWI EGSSRTTGNG
     YITSYNDSWQ HDWAYWANYL AARKMKLGVY YNPLWVHRAA VEDASKTVLG RPDVKIADLV
     VPGDFFARDI GGNQLYWLDV TKSGAKEYVQ GYVRYFKDLG VPYLRIDFLS WYEDGRDANI
     GQVNAPHGRA NYELALSWIN EAAGEDMEVS LVMPHMFQDG SAELANGDLV RINADADKGG
     WDRLSGMRQN WQDAWPNWAN PFCGFTGWSH RNGRGQLILD GDFMRASTFA SDEERKTMMN
     LMVAAGSPLA IADTYQQIGN NAWVYTNKEV LQLNADGLVG KPLYRSATPF SKDPGSRDTE
     RWAGQLPDGS WGVALFNRSD TETVTKTIDF AKDLGLATGG NVRDLWEHRN LGMDSRATAA
     LAPHASAIFR VTPPKMHGTT RYPAAFAAWG GGAGFNNNHP GYDGNGFVDG LQAGSGSADP
     LVTFAVQVPH RAATPSGYRY ANATDDNTTS KTTTKKANPE KADRSTVDGP VHVSFPGLAT
     WDTWGVAAGT ITLDAGLNLV TIGRGATDKG AINLNWIELD M
//