ID A0A0C1N3S6_9CYAN Unreviewed; 686 AA.
AC A0A0C1N3S6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glycogen debranching protein {ECO:0000313|EMBL:KAF3889494.1, ECO:0000313|EMBL:KIE07096.1};
GN Name=glgX {ECO:0000313|EMBL:KAF3889494.1};
GN ORFNames=DA73_0238580 {ECO:0000313|EMBL:KIE07096.1}, DA73_0400031460
GN {ECO:0000313|EMBL:KAF3889494.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE07096.1};
RN [1] {ECO:0000313|EMBL:KIE07096.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE07096.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3889494.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3889494.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
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:KIE07096.1}.
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DR EMBL; JHEG04000001; KAF3889494.1; -; Genomic_DNA.
DR EMBL; JHEG02000059; KIE07096.1; -; Genomic_DNA.
DR RefSeq; WP_038085962.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1N3S6; -.
DR STRING; 1479485.DA73_0238580; -.
DR OrthoDB; 434929at2; -.
DR Proteomes; UP000029738; 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; 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:UP000029738};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 158..565
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 686 AA; 77376 MW; DA048FB2D1DACBC2 CRC64;
MTVDVLPGKS FPIGATIRDG GVNFCLFSRD CTAIELLLFD RPNDPQPSHV IPLDPKQNKT
AHYWHVFVPG IGAGQVYAYR GHGLFAPERG LRCDGDKVLL DPYTKAIANW ENYSRQAASQ
PGDNCARALR SVVIDSSAYD WEDDAPPKTR YNRTIIYELH VGAFTQHPNS GVSPEKRGTY
AGLIEKIPYL QELGITAVEL LPAHQFDRED ARPGLKNYWG YSPIAFFAPH VGYSSCADPF
SPVNEFRDMV KALHRAGIEV ILDVVFNHTA EGDERGPTLS FRGLSNWDYY ILGDNRATYR
NYSGCGNTFK ANSVAGNNLV LDCLRYWVSE MHVDGFRFDL AAVLARGAAG QLLTRPPALL
MIDADPVLAG TKLIAEAWDA EGLYLVGAFV GERFAEWNGP YRDDVRRFVK SDVGMVKALA
NRIMASPDIY SQPNREPHRS INFITCHDGF TLNDLVSYND KHNQANGEDN CDGTNANYSW
NCNIEGETRD LAVHQLRLCQ IKNFLTILFV SQGTPMLLMG DEVRRSQQGN NNAYCQDNEL
SWFDWSAIDK HCEVLRFTQK LISLTQSLKI FHQDRILAVS YGSHQPHIIW HGTQLGQPDW
SYESHSLAFT LRHPKFHEHL YVILNAYWES LAFELPLLEN GYKWYRIVDT ALPSPEDFCD
LQTALPVEKE TYQAQGRSTV VLMAHH
//
