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Database: UniProt
Entry: A0A1Z3HQR3_9CYAN
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Original site: A0A1Z3HQR3_9CYAN 
ID   A0A1Z3HQR3_9CYAN        Unreviewed;       695 AA.
AC   A0A1Z3HQR3;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glycogen debranching enzyme {ECO:0000313|EMBL:ASC72467.1};
GN   ORFNames=XM38_034240 {ECO:0000313|EMBL:ASC72467.1};
OS   Halomicronema hongdechloris C2206.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nodosilineales; Nodosilineaceae;
OC   Halomicronema.
OX   NCBI_TaxID=1641165 {ECO:0000313|EMBL:ASC72467.1, ECO:0000313|Proteomes:UP000191901};
RN   [1] {ECO:0000313|EMBL:ASC72467.1, ECO:0000313|Proteomes:UP000191901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C2206 {ECO:0000313|EMBL:ASC72467.1,
RC   ECO:0000313|Proteomes:UP000191901};
RX   PubMed=26514405; DOI=10.1016/j.bbabio.2015.10.009;
RA   Li Y., Lin Y., Garvey C.J., Birch D., Corkery R.W., Loughlin P.C.,
RA   Scheer H., Willows R.D., Chen M.;
RT   "Characterization of red-shifted phycobilisomes isolated from the
RT   chlorophyll f-containing cyanobacterium Halomicronema hongdechloris.";
RL   Biochim. Biophys. Acta 1857:107-114(2016).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|ARBA:ARBA00004229}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; CP021983; ASC72467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z3HQR3; -.
DR   STRING; 1641165.XM38_20595; -.
DR   KEGG; hhg:XM38_034240; -.
DR   OrthoDB; 9761875at2; -.
DR   Proteomes; UP000191901; Chromosome.
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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000191901};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          164..571
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          469..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  78439 MW;  A378B2727DCE43B3 CRC64;
     MGTAYTHHHT IQPGHSFPLG ATVTPEGVNF CVYSKEATAI ELLLFADEQA DYPSQIIPLD
     PQHHRTSFYW HVLVPGLGHG QVYAYRAYGV FCPERGHRFD ADKVLLDPYS RAVVGHDRYN
     REAARYPGDN CSQALRGVVV DTSRYDWEGD EPLRIPYATS VIYEMHVGGF TRHPNSGVTA
     AKRGTFAGVI EKIPYLKQLG ITAVELLPIH QFDDQDVPPP RKNYWGYSTI AFFAPHQAYS
     CRQDPLGPVD EFRDMVKALH QAGIEVILDV VFNHTAEGNH NGPTLSFRGL DNETYYLLQE
     NRADYANYSG CGNTVKASHA VAGRLIIDCL RYWVSEMHVD GFRFDLASVL SRNLYGHPVD
     DPPILWSIES DPILAGTKLI AEAWDAAGLY QVGSFIGDRF AEWNGPFRDD VRRFVKSDSG
     SVKPLAERII GSPDIYQQPG REPNRSIHFV TCHDGFTLTD LVSYTHKHNQ ANGEDSRDGT
     DANDSWNCGQ EGPTQDPEIE ALRQRQIKNC LTILFFSQGT PMLLMGDEVR RSQGGNNNAY
     CQDNEISWFD WDGLEKHADL LRFTRDLIGL IQRLQIFRIT HSLMVTEHWV KQPHIVWHGV
     NLGQPDWSHD SHSLAFTLRY PAYDEQLHVM LNAFWQPLPF QLPPLRPGDH WHHLVNTAKP
     PPQDLTLPGQ GQAITTPLYE VSCRSAVVVI AQRAQ
//
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