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Entry: A0A091P1S7_HALAL
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ID   A0A091P1S7_HALAL        Unreviewed;      1504 AA.
AC   A0A091P1S7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Glycogen debranching enzyme {ECO:0000256|ARBA:ARBA00020723};
DE            EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560};
DE            EC=3.2.1.33 {ECO:0000256|ARBA:ARBA00012778};
DE   AltName: Full=Glycogen debrancher {ECO:0000256|ARBA:ARBA00031477};
DE   Flags: Fragment;
GN   Name=Agl {ECO:0000313|EMBL:NWZ58108.1};
GN   ORFNames=HALALB_R01368 {ECO:0000313|EMBL:NWZ58108.1}, N329_10863
GN   {ECO:0000313|EMBL:KFQ01214.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ01214.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ01214.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ01214.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NWZ58108.1, ECO:0000313|Proteomes:UP000585422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUT-0040 {ECO:0000313|EMBL:NWZ58108.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:NWZ58108.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-
CC       alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase
CC       in glycogen degradation. {ECO:0000256|ARBA:ARBA00003530}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in
CC         glycogen phosphorylase limit dextrin.; EC=3.2.1.33;
CC         Evidence={ECO:0000256|ARBA:ARBA00000927};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC         position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC         glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC       {ECO:0000256|ARBA:ARBA00025780}.
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DR   EMBL; KK649888; KFQ01214.1; -; Genomic_DNA.
DR   EMBL; VZSQ01000254; NWZ58108.1; -; Genomic_DNA.
DR   Proteomes; UP000054379; Unassembled WGS sequence.
DR   Proteomes; UP000585422; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005980; P:glycogen catabolic process; IEA:InterPro.
DR   CDD; cd11327; AmyAc_Glg_debranch_2; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR010401; AGL/Gdb1.
DR   InterPro; IPR032788; AGL_central.
DR   InterPro; IPR029436; AGL_euk_N.
DR   InterPro; IPR032792; AGL_glucanoTrfase.
DR   InterPro; IPR032790; GDE_C.
DR   InterPro; IPR006421; Glycogen_debranch_met.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   NCBIfam; TIGR01531; glyc_debranch; 1.
DR   PANTHER; PTHR10569; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   PANTHER; PTHR10569:SF2; GLYCOGEN DEBRANCHING ENZYME; 1.
DR   Pfam; PF06202; GDE_C; 1.
DR   Pfam; PF14701; hDGE_amylase; 1.
DR   Pfam; PF14702; hGDE_central; 1.
DR   Pfam; PF14699; hGDE_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..88
FT                   /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14699"
FT   DOMAIN          94..523
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          668..946
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          1045..1499
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ01214.1"
FT   NON_TER         1504
FT                   /evidence="ECO:0000313|EMBL:KFQ01214.1"
SQ   SEQUENCE   1504 AA;  170941 MW;  30A2CD122BA9D641 CRC64;
     GFELQFRLGP TLQGKPVTVY TNYPASGEVF DRHKFRTLSW HNPTGKEDDS DKYCKLDLQI
     SGSYQYYFSL GNEKSGGGYI VVDPILHVGA DNHVLPLDCV TLQTFLAKCL GPFHEWEDRL
     KVAKETGYNM IHFTPLQKLG LSRSCYSLAD QLEVNPEFSS HNKKCTWSDI GALVEKMKNE
     WNMLCITDVV YNHTATNSEW LRMHPECGYN LVNSPHLKPA WVLDRALWHL TCMVADGKYA
     AKGVPSLIEN DHHLNCIRKL IWEDVYPKIK LWEFFQVDVN KAVQQFKSLL TEGKVSTKSD
     PNEHLQIVQD PDYRRFGCTV DMNIALATFI PHSNGPAAIE ECCNWFRKRI EELNAEQYRQ
     TNHHQEQAVN CLVGTVVYER LAGDGPKLGP ISRKNPLVTR YFTYPFKELT VEEEEAMIHQ
     PDKACYFMAH NGWVMGDDPL RNFAEPGSNV YLRRELICWG DSVKLRYGNK PEDCPYLWAH
     MKKYTEITAK YFHGVRLDNC HSTPIHVAEY MLDTARKLRA DLYVVAELFT GNEELDNIFV
     NRLGITSLIR EAMTAYNSHE EGRLVYRFGG EPVGSFVQPR LRPLMPAIAH ALFMDITHDN
     ECPIQHRSAY DALPSAMIVS MACCATGSTK GYDELVPHQI SVVSEERFYA KWNPATHLTS
     GEVNFQTGIL AGRLAINRLH QELGAKGFNQ ARSEDQVDED IVAVTRHCPN THQSVVAVSR
     TAFRDPKTSF YSKEVPEMCI PGKIEEVVLE ARTIERNASP YKKDERFING LPNFTMELRE
     HIQIKDSKII KQAGTAIKGP NEFVQEIEFE KLTPGSVIVF RVSLDPKAQE AVGVLRNHLI
     QFSPHFKSGS LPDDHSAPIL KTLFSSIASK LTLADLNQVL YRCEAEEQED GGGCYNIPNW
     SPLKYAGLQG LMSVMADIRP KNDLGHPFCD NLRSGDWMID YVSNRLISRA GACAEVGKWL
     KAMFVYLKRI PRYLIPCYFD AILVGAYTTL LDVGWHHMSS FVQNGSTFVK HLSLGSVQMC
     GIGKYSCLPD LSPSLHDVPY RLNEITNEKE QCCVSLAAGL PHFSSGIFRS WGRDTFIALR
     GLMLVTGRYL EARNIILAFG GTLRHGLIPN LLGQGTHARY NCRDAVWWWL QCIQDYCKIV
     PNGLDILRCP VSRMYPRDDS SPQPAGTMDQ PLYEVIQEAM QRHMEGINFR ERNAGPQIDQ
     NMRDEGFNVT AGVDNETGFV FGGNRFNCGT WMDKMGESDR ARNRGIPATP RDGSAVEIVG
     LCKSAVRWLL DLSGKNVFPF RGVTVKRHEK EETITYDEWN RKIQGHFERL FFVSENPADP
     NEKHPNLVHK RGIYKDSYGA SSPWCDYQLR PNFTIAMVVA PELFTPERAW KALQIAEEKL
     LGPLGMKTLD PDDMVYCGVY DNALDNDNYN VARGFNYHQG PEWLWPIGYF LRAKLYFSKL
     IGPEIYAKTV VMIKNVLSRH YVHLERSSWK GLPELTNENG QYCPFSCETQ AWSIGVILEI
     LYDL
//
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