ID   C4LI82_CORK4            Unreviewed;       771 AA.
AC   C4LI82;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Putative glycogen debranching enzyme {ECO:0000313|EMBL:ACR17537.1};
GN   OrderedLocusNames=ckrop_0780 {ECO:0000313|EMBL:ACR17537.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 /
OS   CCUG 35717).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR17537.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR17537.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I., Goetker S.,
RA   Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium that
RT   lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; CP001620; ACR17537.1; -; Genomic_DNA.
DR   RefSeq; WP_012731424.1; NC_012704.1.
DR   AlphaFoldDB; C4LI82; -.
DR   STRING; 645127.ckrop_0780; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; ckp:ckrop_0780; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_011725_1_1_11; -.
DR   OrthoDB; 3236218at2; -.
DR   Proteomes; UP000001473; Chromosome.
DR   GO; GO:0004133; F:glycogen debranching enzyme activity; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR   CDD; cd11326; AmyAc_Glg_debranch; 1.
DR   CDD; cd02856; E_set_GDE_Isoamylase_N; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; IPR011837; Glycogen_debranch_GlgX.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   NCBIfam; TIGR02100; glgX_debranch; 1.
DR   PANTHER; PTHR43002; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR43002:SF1; ISOAMYLASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF02922; CBM_48; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001473}.
FT   DOMAIN          216..618
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   771 AA;  86984 MW;  3547FB473B3E71C0 CRC64;
     MKNTQEQASE KIVDNDHEAP TISGQATSPA TDDATANDGS SATSSDNAPD LVVWPGNSYP
     LGSTYDGSGT NFALFSEVAD KVELCLIDSD GAETRIEMRE VDAHIWHCYL PGIIPGQRYG
     YRVHGPWDPH QGLRCDPSKI LLDPYAKAFD GKFDGDASLF SYDIDNPDER NTDDSLGHTM
     LSVVINPYFD WGSDRLPRHP MNKTVVYEAH VKGMTMTHPD VPENYRGTYA GLAHPSIVKY
     LKDLGVTAIE LMPIHQFYQD DRLHELGLSN YWGYNTFGFL APHQDYAAAK KPGAAVSEFK
     NMVRAFHDND IEVILDVVYN HTAEGNHMGP TLSFRGIDNA AYYRLVDDDR QHYMDYTGTG
     NSLNVRHPHT LQLIMDSLRY WVTEMHIDGF RFDLASTLAR ELHDVDRLSA FFDLVQQDPI
     VSQVKLIAEP WDVGEGGYQV GNFPAIWSEW NGMYRDTVRD FWRGEPATLG EFASRLTGSS
     DLYAANDRRP TASINFVTAH DGFTLHDLVS YNEKHNEANK EDNRDGESHN RSWNCGVEGP
     TDDPDIIQLR GRQIRNFLTT LLLSQGTPMI CHGDEMGRTQ NGNNNVYCQD SELSWVDWSQ
     ATDNKDLIDF TRRLIELRND HPVFRRRRFL AGGPLGYDVQ DRDIAWMTPA GTLMTTADWD
     HDFGRSLMVH LGGEAIAEPD EQGQKIFDDS FILCFNAHHE RIDFTLPKDD AVKASRDPED
     TDPSRLWSVV VDTSLPTGFS EDDPDVYKPE STVPVENRSV VVLCRRRRHS A
//