ID   C1A0S9_RHOE4            Unreviewed;       779 AA.
AC   C1A0S9;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Probable glycogen debranching enzyme {ECO:0000313|EMBL:BAH34214.1};
DE            EC=3.2.1.- {ECO:0000313|EMBL:BAH34214.1};
GN   Name=glgX {ECO:0000313|EMBL:BAH34214.1};
GN   OrderedLocusNames=RER_35060 {ECO:0000313|EMBL:BAH34214.1};
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH34214.1, ECO:0000313|Proteomes:UP000002204};
RN   [1] {ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAH34214.1, ECO:0000313|Proteomes:UP000002204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX   PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA   Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA   Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA   Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT   "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT   strain PR4.";
RL   Environ. Microbiol. 8:334-346(2006).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; AP008957; BAH34214.1; -; Genomic_DNA.
DR   RefSeq; WP_020908048.1; NC_012490.1.
DR   AlphaFoldDB; C1A0S9; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; rer:RER_35060; -.
DR   PATRIC; fig|234621.6.peg.4022; -.
DR   eggNOG; COG1523; Bacteria.
DR   HOGENOM; CLU_011725_1_1_11; -.
DR   Proteomes; UP000002204; 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   Glycosidase {ECO:0000313|EMBL:BAH34214.1};
KW   Hydrolase {ECO:0000313|EMBL:BAH34214.1}.
FT   DOMAIN          235..645
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          128..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..186
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   779 AA;  86315 MW;  3948C3DC5ACE42BF CRC64;
     MDQPPSAPSA TPIPVWPGSA YPLGATYDGA GTNFSLFSEV AEAVELCLIA KDGTETRIRM
     DEVDGYVWHA YLPSVSPGQR YGYRVHGPYD PAAGLRCDPS KLLLDPYGKA FDGDFDGDRS
     LFSYDVESAA DPEPAGDDET PAVEPEEATD ETSSEAESGE VGLEDESPTD DQESDESLDP
     EPFDPEPLVD EPATIPFPQH DSLGHTMSTV VINPFFDWAS DRSPKRPYHE TVIYEAHVKG
     MTATHPGVPE ELRGTYAGLA HPVIIEHLTN LGVTAIELMP VHQFMHDQVL LDQGLRNYWG
     YNTFGFLAPH TDYSSAAKPD AAVAEFKAMV RSFHQAGIEV ILDVVYNHTA EGNHMGPTIS
     FRGIDNAAYY RLVDGDEAHY MDYTGTGNSL NARHPHTLQL IMDSLRYWVT EMHVDGFRFD
     LASTLARELH DVDRLSAFFD LVQQDPIVSQ VKLIAEPWDV GEGGYQVGNF PGLWTEWNGK
     YRDTVRDYWR GEPATLGEFA SRLTGSSDLY EATGRRPGAS INFVIAHDGF TLHDLVSYNE
     KHNEANGENN NDGESHNRSW NCGVEGPTDD PEILELRGRQ SRNILATLML SQGTPMLAHG
     DEMGRTQQGN NNVYCQDSEL SWMDWTLAET NADLVEFTKR AIALRAKNPV FRRRRFFEGR
     PIRSGDQGRD IAWLTPSGEE MTPADWDSGF GKSLAVFLNG DAIPEPNYRG ERVTGDSFLL
     CFNAHYEDLE FSTPNADYAS EWTVVLDTSV PTGESDTVIK AGTTLDVKAR ALTVLRRTA
//