IMGH_KRIFD
ID IMGH_KRIFD Reviewed; 385 AA.
AC D2PPM8;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Isomaltose glucohydrolase {ECO:0000303|PubMed:27302067};
DE EC=3.2.1.205 {ECO:0000269|PubMed:27302067};
GN OrderedLocusNames=Kfla_1896 {ECO:0000312|EMBL:ADB30990.1};
OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC Bacteria; Actinobacteria; Propionibacteriales; Kribbellaceae; Kribbella.
OX NCBI_TaxID=479435;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000312|Proteomes:UP000007967};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Kribbella flavida DSM 17836.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP GLU-178 AND GLU-335, SUBCELLULAR LOCATION, ACTIVE SITE, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399;
RX PubMed=27302067; DOI=10.1074/jbc.m116.727305;
RA Tagami T., Miyano E., Sadahiro J., Okuyama M., Iwasaki T., Kimura A.;
RT "Two novel glycoside hydrolases responsible for the catabolism of cyclobis-
RT (1->6)-alpha-nigerosyl.";
RL J. Biol. Chem. 291:16438-16447(2016).
CC -!- FUNCTION: Involved in the intracellular degradation of the cyclic
CC tetrasaccharide cyclobis-(1-6)-alpha-nigerosyl (CNN) formed
CC extracellularly from starch. Catalyzes the hydrolysis of alpha-1,6-
CC glucosidic linkage from the non-reducing end of isomaltose to yield
CC beta-D-glucose and D-glucose. Can also act on panose and isomaltotriose
CC at a lower rate. It displays low or no activity toward CNN and the
CC general GH15 enzyme substrates such as maltose, soluble starch or
CC dextran. {ECO:0000269|PubMed:27302067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isomaltose = beta-D-glucose + D-glucose;
CC Xref=Rhea:RHEA:52752, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15903, ChEBI:CHEBI:28189; EC=3.2.1.205;
CC Evidence={ECO:0000269|PubMed:27302067};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.68 mM for panose {ECO:0000269|PubMed:27302067};
CC KM=2.38 mM for isomaltose {ECO:0000269|PubMed:27302067};
CC KM=4.36 mM for isomaltotriose {ECO:0000269|PubMed:27302067};
CC Note=kcat is 11.4 sec(-1) for isomaltose as substrate. kcat is 1.17
CC sec(-1) for panose as substrate. kcat is 1.07 sec(-1) for
CC isomaltotriose as substrate. {ECO:0000269|PubMed:27302067};
CC pH dependence:
CC Optimum pH is 6.7. Stable between pH 6.5 and 11.2.
CC {ECO:0000269|PubMed:27302067};
CC Temperature dependence:
CC Optimum temperature is under 35 degrees Celsius.
CC {ECO:0000269|PubMed:27302067};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:27302067}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. {ECO:0000305}.
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DR EMBL; CP001736; ADB30990.1; -; Genomic_DNA.
DR PDB; 5Z3A; X-ray; 1.40 A; A=1-385.
DR PDB; 5Z3B; X-ray; 1.25 A; A=1-385.
DR PDB; 5Z3C; X-ray; 1.60 A; A=1-385.
DR PDB; 5Z3D; X-ray; 1.25 A; A=1-385.
DR PDB; 5Z3E; X-ray; 1.10 A; A=1-385.
DR PDB; 5Z3F; X-ray; 1.10 A; A=1-385.
DR PDB; 7C24; X-ray; 1.71 A; A=1-385.
DR PDB; 7C25; X-ray; 1.50 A; A=1-385.
DR PDB; 7C26; X-ray; 1.80 A; A=1-385.
DR PDB; 7C27; X-ray; 1.91 A; A=1-385.
DR PDBsum; 5Z3A; -.
DR PDBsum; 5Z3B; -.
DR PDBsum; 5Z3C; -.
DR PDBsum; 5Z3D; -.
DR PDBsum; 5Z3E; -.
DR PDBsum; 5Z3F; -.
DR PDBsum; 7C24; -.
DR PDBsum; 7C25; -.
DR PDBsum; 7C26; -.
DR PDBsum; 7C27; -.
DR AlphaFoldDB; D2PPM8; -.
DR SMR; D2PPM8; -.
DR STRING; 479435.Kfla_1896; -.
DR CAZy; GH15; Glycoside Hydrolase Family 15.
DR EnsemblBacteria; ADB30990; ADB30990; Kfla_1896.
DR KEGG; kfl:Kfla_1896; -.
DR eggNOG; COG3387; Bacteria.
DR HOGENOM; CLU_801178_0_0_11; -.
DR OMA; NGMWEEN; -.
DR BioCyc; MetaCyc:MON-20072; -.
DR BRENDA; 3.2.1.205; 14106.
DR Proteomes; UP000007967; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..385
FT /note="Isomaltose glucohydrolase"
FT /id="PRO_0000443931"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10051"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27302067"
FT ACT_SITE 335
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27302067"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P69327"
FT MUTAGEN 178
FT /note="E->A: Loss of glucohydrolase activity."
FT /evidence="ECO:0000269|PubMed:27302067"
FT MUTAGEN 335
FT /note="E->A: Loss of glucohydrolase activity."
FT /evidence="ECO:0000269|PubMed:27302067"
FT HELIX 12..32
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 88..99
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:5Z3E"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:5Z3E"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 131..147
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 211..228
FT /evidence="ECO:0007829|PDB:5Z3E"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:5Z3E"
FT TURN 252..255
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:5Z3E"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5Z3F"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 313..324
FT /evidence="ECO:0007829|PDB:5Z3E"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:5Z3E"
FT HELIX 362..374
FT /evidence="ECO:0007829|PDB:5Z3E"
SQ SEQUENCE 385 AA; 41807 MW; 4E1AD872D55E090A CRC64;
MTTSARDTGL DSHELARLHE LARHSHAVIT RHQDAGGAYP AAPTFSAYRG YAWLRDGSFT
AEGISRYGDV ASAGRFHDWV DGVLRRRRGQ VDDLLAAVDR GEVPSNEGML PTRFTFDGND
GSDPWWDFQT DGYGMWLWSV VTHAARHGLD LERWRAGIDV AVDYLLAFWD RPCYDWWEEH
VEHRHVSTLG AIHGGLVAVG TCAALRSAPW SAATLQVAAR IRSLVSAEGV VDGHLVKWLG
SSAVDGSLPA CVVPFGLVPP DDDVAAMTRA AVAKDLDVDG GVHRFAADVF YGGGQWILLS
ALLGWNLAAA GDTAGALRHL RWIADQADAD GDLPEQVPHH LLHPGSRAEW VARWGTVATP
LLWSHGMYLI LADELGLLPP AAKDA
