ID   A0A2R5FV56_NOSCO        Unreviewed;       708 AA.
AC   A0A2R5FV56;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glycogen debranching enzyme GlgX {ECO:0000313|EMBL:GBG20083.1};
GN   ORFNames=NIES4072_37520 {ECO:0000313|EMBL:GBG20083.1};
OS   Nostoc commune NIES-4072.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2005467 {ECO:0000313|EMBL:GBG20083.1, ECO:0000313|Proteomes:UP000245124};
RN   [1] {ECO:0000313|EMBL:GBG20083.1, ECO:0000313|Proteomes:UP000245124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-4072 {ECO:0000313|EMBL:GBG20083.1,
RC   ECO:0000313|Proteomes:UP000245124};
RA   Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT   "Genome sequencing of cyanobaciteial culture collection at National
RT   Institute for Environmental Studies (NIES).";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GBG20083.1}.
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DR   EMBL; BDUD01000001; GBG20083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R5FV56; -.
DR   OrthoDB; 434929at2; -.
DR   Proteomes; UP000245124; Unassembled WGS sequence.
DR   GO; GO:0004133; F:glycogen debranching enzyme activity; IEA:InterPro.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245124};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          163..574
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          472..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   708 AA;  80568 MW;  58DBF2254843A4CA CRC64;
     MYIAVWPGNV YPLGATWDGK GTNFALFSEN ATSVELCLFD ADNDEIRLPL TEKNNFVWHA
     YLPGVGPGQR YGFRVHGPWA PELGHRFNPN KLLIDPYAKA IDGEIIDNPA NFGYSLDAPE
     QDLAFSDLDN AEIMPKCIVV DQSFDWGDDK LLSIPWHETI IYETHVKGFT KLHPEIPEEL
     RGTYAGLAHP AAIQYLQQLG ITSVELMPVH HFLSSPGFLV DKGLKNYWGY DSINYLTPYS
     GYSASGSLGQ QVTEFKQMVK DLHAAGIEVI LDVVYNHTGE GNHLGPTLSL RGIDNAVYYR
     LVKDNSRYYM DFTGCGNSLN VRHAQVLKLI MDSLRYWVTE MHVDGFRFDL ASALARELYE
     VDNLAAFFDI IHQDPVLADV KLIAEPWDLG EGGYQVGNFP LRWSEWNGRY RDTVRDFWRG
     EDDSLGQFAY CFTGSPDLYQ ANGRNPSASI NFITAHDGFT LNDLVSYNEK HNQANGEDSR
     DGESHNRSWN CGVEGETDDP DVIRLRERQR RNFLATLMLS QGVPMLLAGD EIGCTQKGNN
     NAYCQDNEIS WRDWSLQKSN SELLDFSREL IDFRHKHPVF RRRKWFQGRP IHGFGINDIG
     WFNADGSEMT EKQWLVSYAK AMEIFLNGEG ILTPGPRGER IIDESFLLFF NAHYETLEFA
     LPNVFQDREW EIVIDTNESR FLSPGKLIMG EQTVPVTDRS IMVLRRLA
//