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Database: UniProt
Entry: W5KD30_ASTMX
LinkDB: W5KD30_ASTMX
Original site: W5KD30_ASTMX 
ID   W5KD30_ASTMX            Unreviewed;      1501 AA.
AC   W5KD30;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 46.
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};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000005491.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000005491.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   STRING; 7994.ENSAMXP00000005491; -.
DR   Ensembl; ENSAMXT00000005491.2; ENSAMXP00000005491.2; ENSAMXG00000005334.2.
DR   eggNOG; KOG3625; Eukaryota.
DR   GeneTree; ENSGT00390000012596; -.
DR   HOGENOM; CLU_001517_2_0_1; -.
DR   InParanoid; W5KD30; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000005334; Expressed in muscle tissue and 14 other cell types or tissues.
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; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_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:UP000018467};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          31..116
FT                   /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14699"
FT   DOMAIN          122..548
FT                   /note="Glycogen debranching enzyme glucanotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF14701"
FT   DOMAIN          694..944
FT                   /note="Glycogen debranching enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF14702"
FT   DOMAIN          1043..1496
FT                   /note="Glycogen debranching enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06202"
SQ   SEQUENCE   1501 AA;  169820 MW;  623AE41BA412F0AE CRC64;
     MSPSKQIRVL VLNDMEKLDR TLFRLEQGFE LQFRLGPTLQ GKNIHVHTNY PAQGEQFDRH
     RFRTLDWINP TGREDDSDKF CSLELQIAGS YQYYFGQGDK DKSGGGYIVV DPMLRVGADN
     HVLPLDCISI QTYLAKCLGP LDEWLDRLRV AKETGYNMIH FTPLQTLGES RSCYSLADQL
     ELNPDFSPPG QNYTWTDVGN LVEKMKKEWD MLCITDVVYN HTAANSVWIQ KHPECGYNLL
     NSPHLRPAWV LDRALWHVTC DIADGKYADR GVPALLQNEH HMNSIRGIFW QDVYPKTKLW
     EFFQVKVEPL VEKFRTLLQN GDKIQTDGKK QLKIIQDPQY NRFGCTVDLN TALEIFVSNG
     PGAIEDCCNW FRKRLEELNA EQFKEVNYHQ EQATNCCMGT VSYERLADHG PKLGPVTRKH
     PLVTRYFTFP FKESPLEQDL LLMDQPDKAC HFLAHNGWVM GDDPLRNFAE PGSNVYIRRE
     LICWGDSVKL RYGKGPEDCP YLWAHMQKYT EITAKYFTGV RLDNCHSTPL HVAEFMLAAA
     RAINPDLYVV AELFTGSEEL DNVFVTRLGI SSLIREALSA GDSHEEGRLV YRYGGEPVGA
     FLQPSLRPLV PSIAHAMFLD ITHDNECPIQ IRSAFDSLPS SAIVSMACCA TGSTRGYDEF
     VPHQISVVSE ERFYQKWNPQ AKPSPPGEVS LQSGIIAGKL ALNRLHQELA AKGFSQVYVD
     QVDEDIVAVT RHCPSSHQSV VAVCRTAFKN PKHHKYSDEV PPMFIPGQWL VQVQKVKNPL
     HGFLKDSTVV KQAGVTSRGR SEFVQEIVFE RLTPGSVIAF RVSLDPTAQE LVGILRTHLI
     QFNPHYAAGS IPDKNAPEIL KTPLKESKLT LADMNVLMFR CDEEEKEDGG GCYSIPGWTT
     LKYGGLQGLL SVMADIRPKN DLGHPFCDNL RQGDWMIDYV SSRLVSHGGT LGEVGQWFQA
     MFGYLKHIPR YLIPCYFDAV LVGAYTTALD ASFKLMSSFV QQGSSFVRQL ALGSIQMCGI
     GRFPALPPLS PALTDVPYRT NSITQQEQQF CVSMAAGLPH FSAGIFRCWG RDTFIALRGL
     LLVTGRHLEA RNIILSFAGT LRHGLIPNLL GEGVSARFNC RDAVWWWLQC IQDYSTIVPN
     GTSILQCPVS RMYPTDDSQP QAPGTVDQPL YDVIHEALQR HMQGIEFRER NAGPQIDRNM
     RDEGFNIVAK VNPDTGFVYG GNRFNCGTWM DKMGESERAR NKGIPATPRD GSAVEIVALC
     KSAVRWLVEL HKQGLFPYDC VTINKDGAKI TVPYADWNRN LQNNFEKMFY VSQDPKDPNE
     KHPELVHKRG IYKDSVGASS PWCDYQLRPN FTIAMVVAPE LFTVERAWEA LNMAEKLLGP
     LGMKTLDPDD MVYCGVYDNS LDNDNYNLAK GFNYHQGPEW LWPVGYFLRA KLYFAKKLGK
     ETYDKTVYLV KNVLSRHYVH LERSPWKGLP ELTNENGQYC SFSCETQAWS IATVLEVLYD
     L
//
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