ID H3DLB9_TETNG Unreviewed; 1534 AA.
AC H3DLB9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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};
GN Name=AGL {ECO:0000313|Ensembl:ENSTNIP00000021317.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000021317.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000021317.1}
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; 99883.ENSTNIP00000021317; -.
DR Ensembl; ENSTNIT00000021552.1; ENSTNIP00000021317.1; ENSTNIG00000018151.1.
DR GeneTree; ENSGT00390000012596; -.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; H3DLB9; -.
DR OMA; YEEGHVH; -.
DR TreeFam; TF300697; -.
DR Proteomes; UP000007303; 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; 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:UP000007303};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 29..114
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 120..551
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 697..975
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1075..1529
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1534 AA; 173289 MW; 08B921057F9D8042 CRC64;
HLKQIRVLML NDKENLQRTL FRLEQGFELQ FRLGPSLQGK KVWVHTNYPL EGQPYRRHKF
RVLEWNNPTG REDDSDKFCS LDLKIAGSYE YYFGHGDTEQ SGGGYIVVDP VLRVGADSHV
LPLDCITIQT YLSKCLGHLD DWPSRLRVAK ESGYNMIHFT PLQTLGESRS CYSLADQLTF
SPEFSPQGQR YTWADVGALV DKLRTDWEML CITDVVYNHT AANSVWIKEH PECGYNLVNS
PHLTPAWVLD RAVWHLTTRV ADGRYSERGL TADITSEAQL NAIRSVLWQD VFPQIKLWEF
FQVHVASALE EFRTRLQNGS KPDHSKTGGR KGLKVVQDPH YRRYGNRVDM DSALETFVPV
SFSPQHIEEC CGCLREKLDE LNKEQHHIVQ QHQEQAVNCI VGNVVYERLA EHGPKLGPVT
RKNPLVTRYF TFPYQDMTLE QELLLLEQPD KACHFLAHNG WVMGDDPLRN FAEPGSNVYL
RRELICWGDS VKLRYGNGPE DCPYLWAHMQ KYTEITAQYF SGVRLDNCHS TPLHVAEYML
DVARRASPNL YVVAELFTGS EELDNVFVTK LGITSLIREA MSAGDSHEEG RLVYRYGGEP
VGAFYQPSLR PLVPSIAHAM FLDVTHDNEC PIQLRSALDS LPSSALVSMA CCATGSTRGY
DELVPHQISV VKEERLYPKW NPTAAPESSS EVGFQTGIIA GKLALNKLHK ELAAQGFIQV
YVDQVDADIV AVTRHCPSTH QSVVSVCRTA FWNPQTHQYD TNVPPMFIPG KIEEVVLEAR
TVERHAGAYK KDEKFINGMP EYHVEIKEHI PLEDSTVVRK AGVTSKGRSE FVQEINFQKL
TPGSVIAFRV SLDPKAQRMV GLLRFYLSQF SPKYRKGSVT EENPPEPLQK PLAQLMSQLT
LADLNVLLFR CDSEEQEDGG GCYSIPGWET LKYAGLQAGL ISVFANVRPS NDLGHPVCAN
LRQGDWLIDY VSNRLVHREG ALAQVGQWLA AMFGYLKHIP RYLIPCYFDA ILVSTYTTAL
DAAYQLMSSF VRNGSTFVRH LALGSIQMCS VGRFPALPPL SAKVEDVPYR VSPITGQKEQ
CCVSLAAGLP HFSAGIFRCW GRDTFIALRG LLLLTGRHVE ARNIILAFAG TLRHGLIPNL
LGEGRCARYN CRDAVWWWLQ CIQDYANSVP QGEEILRCPV TRMYPTDDCE PCRPGELEQP
LYEVIQEALQ RHLQGISFRE RNAGPKIDMN MRDASSGFNV SVKVDVDTGF VSGGNRFNCG
TWMDKMGESD RARNKGMPAT PRDGAAVEIV GLSKSAVRWL VELHAKGLFP YAGAKVRRDG
QEVFVSYSQW NQQLQQTFEL AFWVSEDPQD PNEKHPELVH KRGIYKDSYG ASSPWCDYQL
RPNFTIAMVV APELFTVERA WTALSVVEKK LLGPLGMKTL DPDDMVYCGV YDNALDNDNY
NRARGFNYHQ GPEWLWPVGY FLRAKLHFAK QLGGDTVRAV TLIKGVVSRH YPHLERSPWK
GLPELTNENG QHCPFSCESQ AWSLATLLEL LHQL
//
