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Database: UniProt
Entry: A0A0D6KC97_9CYAN
LinkDB: A0A0D6KC97_9CYAN
Original site: A0A0D6KC97_9CYAN 
ID   A0A0D6KC97_9CYAN        Unreviewed;       706 AA.
AC   A0A0D6KC97;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Glycogen debranching enzyme GlgX {ECO:0000313|EMBL:EKE97012.1};
GN   ORFNames=FDUTEX481_06076 {ECO:0000313|EMBL:EKE97012.1};
OS   Tolypothrix sp. PCC 7601.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE97012.1, ECO:0000313|Proteomes:UP000032761};
RN   [1] {ECO:0000313|EMBL:EKE97012.1, ECO:0000313|Proteomes:UP000032761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX   PubMed=25953173;
RA   Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA   Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA   Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA   Kehoe D.M., Weinstock G.M.;
RT   "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT   Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT   PCC 7601.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
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:EKE97012.1}.
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DR   EMBL; AGCR01000124; EKE97012.1; -; Genomic_DNA.
DR   RefSeq; WP_045874488.1; NZ_JH930377.1.
DR   AlphaFoldDB; A0A0D6KC97; -.
DR   STRING; 1188.FDUTEX481_06076; -.
DR   PATRIC; fig|1188.3.peg.9473; -.
DR   HOGENOM; CLU_011725_1_1_3; -.
DR   OrthoDB; 434929at2; -.
DR   Proteomes; UP000032761; 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:0019156; F:isoamylase activity; IEA:UniProt.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR   CDD; cd11326; AmyAc_Glg_debranch; 1.
DR   CDD; cd11234; E_set_GDE_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; 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   InterPro; IPR048650; ISOA1-3-like_C.
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; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   Pfam; PF21156; ISOA1-3_C; 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   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          164..577
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          476..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..494
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   706 AA;  80084 MW;  4F610B93308B6BF6 CRC64;
     MERIDIHPTH TYEGFKLRNG KPFPFGATLV PGGVNFSIFS SQATSCTLVL FKKHDQKPLV
     EIPFPEEFRI GNVYCMVVFD LDYENLEYGY RMDGPKNFRE GHWFDKSKIL MDPYAKIIGG
     RDVWGVTPDW NDIYHHRARI AFDDFDWEDD RPLEIPPSDQ VIYEMHVRSF TRHPSSGVKD
     NHKGTFAGIR EKIPYLKELG VNAVELMPIY EFDEFENSRP NPQTGETLYN YWGYSTVGFF
     APKAGYAATG KFGMQVDELK SLVKELHKNG IEVILDVVFN HTAEGNEHGP TISFRGIDNK
     TYYMLTPEGY YYNFSGTGNT LNCNNPVVRG IVLDCLRYWA SEYHIDGFRF DLAAILGRDP
     WGAPLANPPL LESLAFDPIL AKCKLIAEAW DAGGLYQVGS FPAYGRWAEW NGKYRDGIRK
     FLKGDGSVGD AAQRLQGSPD LYAWSGRAPA TSINFITAHD GFTMMDLVSY NGKHNEANGE
     NNNDGSNDND SWNCGWEGPT DDPGINALRH RQIKNAVALL MVSQGVPMIL MGDEVGRTQK
     GNNNTYCHDN DLNWLDWTLL EKNADLFKFF KHCIAFRNAH PVLRNEWHFQ NRDYVGSGYA
     DITWHGTQAW NADWSDSCKT LAFMLCGKHA KQGTVEDNYI YVAMNMHWES LWFEIPRLHP
     GMKWHIFANT GANPAEASWE PGKEPVLENQ AALLMGDRSV AILVGK
//
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