AIMA_KRIFD
ID AIMA_KRIFD Reviewed; 723 AA.
AC D2PPM7;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=1,3-alpha-isomaltosidase {ECO:0000303|PubMed:27302067};
DE EC=3.2.1.204 {ECO:0000269|PubMed:27302067};
GN OrderedLocusNames=Kfla_1895 {ECO:0000312|EMBL:ADB30989.1};
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 ASP-451 AND ASP-516, 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 the alpha-1,3-
CC glucosidic linkage of cyclobis-(1-6)-alpha-nigerosyl (CNN) to yield
CC isomaltose via a possible linear tetrasaccharide. It has a strong
CC preference for the alpha-(1-3)-isomaltosyl moiety.
CC {ECO:0000269|PubMed:27302067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclobis-(1->3)-alpha-D-isomaltosyl + 2 H2O = 2 isomaltose;
CC Xref=Rhea:RHEA:24844, ChEBI:CHEBI:15377, ChEBI:CHEBI:28189,
CC ChEBI:CHEBI:136822; EC=3.2.1.204;
CC Evidence={ECO:0000269|PubMed:27302067};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.63 mM for cyclobis-(1-6)-alpha-nigerosyl (CNN)
CC {ECO:0000269|PubMed:27302067};
CC Note=kcat is 22.3 sec(-1) for cyclobis-(1-6)-alpha-nigerosyl (CNN) as
CC substrate. {ECO:0000269|PubMed:27302067};
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:27302067};
CC Temperature dependence:
CC Optimum temperature is under 41 degrees Celsius.
CC {ECO:0000269|PubMed:27302067};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:27302067}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family. {ECO:0000305}.
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DR EMBL; CP001736; ADB30989.1; -; Genomic_DNA.
DR RefSeq; WP_012919545.1; NC_013729.1.
DR PDB; 5X3I; X-ray; 2.10 A; A/B=1-723.
DR PDB; 5X3J; X-ray; 2.30 A; A/B=1-723.
DR PDB; 5X3K; X-ray; 2.50 A; A/B=1-723.
DR PDBsum; 5X3I; -.
DR PDBsum; 5X3J; -.
DR PDBsum; 5X3K; -.
DR AlphaFoldDB; D2PPM7; -.
DR SMR; D2PPM7; -.
DR STRING; 479435.Kfla_1895; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR EnsemblBacteria; ADB30989; ADB30989; Kfla_1895.
DR KEGG; kfl:Kfla_1895; -.
DR eggNOG; COG1501; Bacteria.
DR HOGENOM; CLU_009658_1_0_11; -.
DR OMA; EWSFDPE; -.
DR OrthoDB; 469334at2; -.
DR BioCyc; MetaCyc:MON-20073; -.
DR BRENDA; 3.2.1.204; 14106.
DR Proteomes; UP000007967; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome.
FT CHAIN 1..723
FT /note="1,3-alpha-isomaltosidase"
FT /id="PRO_0000443932"
FT ACT_SITE 451
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:27302067"
FT ACT_SITE 454
FT /evidence="ECO:0000250|UniProtKB:P31434"
FT ACT_SITE 516
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27302067"
FT BINDING 581
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32138"
FT MUTAGEN 451
FT /note="D->A: Loss of isomaltosidase activity."
FT /evidence="ECO:0000269|PubMed:27302067"
FT MUTAGEN 516
FT /note="D->A: Loss of isomaltosidase activity."
FT /evidence="ECO:0000269|PubMed:27302067"
FT TURN 6..9
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:5X3J"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5X3J"
FT HELIX 76..81
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 201..210
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 355..364
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 447..450
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:5X3I"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 476..490
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 521..536
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 541..545
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 556..566
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 590..597
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 602..630
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 646..650
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:5X3I"
FT TURN 658..660
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 672..678
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:5X3I"
FT TURN 686..688
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 694..700
FT /evidence="ECO:0007829|PDB:5X3I"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 712..714
FT /evidence="ECO:0007829|PDB:5X3I"
FT HELIX 715..722
FT /evidence="ECO:0007829|PDB:5X3I"
SQ SEQUENCE 723 AA; 80101 MW; 69A093BB5820BE56 CRC64;
MIKHRPHGIE HPYAVSPDQR VPVLPLAGEP VLLGVVAPEA DRVVCEWGTL ELPLSATSAA
AADAAALAGG EGHLSEAQAK SLGADGAWSV QTPPLAEPVK YRFHAHRGGA AESTEWFEVS
PAVWTADGVG EVRGGGERVR GVEWLVSSQG VHRGRFRLQL QDGDRLVGFG ERYDALDQRG
RELDAVVFEQ YKAQGVHGRT YLPMPFAHVV GADGNGWGFH VRTSRRTWYS SAGNELTVEV
ALGDEPVVDL AIYEGDPATV LTGFLDEVGR AEELPGWVFR LWASGNEWNT QQLVTARMDT
HRDLAIPVGA VVIEAWSDEQ GITIWRDAVY AVTEDGSAHR AEDFSYRPDG AWPDPKAMID
ELHARGIKVI LWQIPLQKTE FSTGQVAADA AAMVRDGHAV LEADGTAYRN RGWWFPQALM
PDLSVQRTRD WWTEKRRYLV EHFDVDGFKT DGGEHAWGHD LVYADGRKGD EGNNLYPVHY
ARAFGDLLRS AGKAPVTFSR AGFTGSQAHG IFWAGDEDST WQAFRSSVTA GLTAASCGIV
YWGWDLAGFS GPVPDAELYL RAAAASAFMP IMQYHSEFNH HQLPLRDRTP WHVAETTGDD
RVVPLFRRFA TLRESLVPYL TEQAARTIAT DRPLMRPLFF DHENDPEIWN HPYQYLLGDE
LLINPVLEPG ATTWTTYLPA GEWIDVWTGD RVPSGLVTRD VPLEVVPVYC RASRWSELQP
VFS
