ID T1EEV2_HELRO Unreviewed; 1530 AA.
AC T1EEV2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=20195104 {ECO:0000313|EnsemblMetazoa:HelroP109597};
GN ORFNames=HELRODRAFT_109597 {ECO:0000313|EMBL:ESO09331.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP109597, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESO09331.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP109597}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) 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 EMBL; AMQM01002938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB095959; ESO09331.1; -; Genomic_DNA.
DR RefSeq; XP_009012424.1; XM_009014176.1.
DR STRING; 6412.T1EEV2; -.
DR EnsemblMetazoa; HelroT109597; HelroP109597; HelroG109597.
DR GeneID; 20195104; -.
DR KEGG; hro:HELRODRAFT_109597; -.
DR CTD; 20195104; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; T1EEV2; -.
DR OMA; YEEGHVH; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IBA:GO_Central.
DR GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000015101};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 31..119
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 125..551
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 697..966
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1070..1519
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1530 AA; 174668 MW; 7CEEE703AEB093A5 CRC64;
MASQSQLRLL VLRHGDMHEA TLYRLERGWK LHFVLDASLT GLPVRLFVNH PLDAKSGPNR
YIYRELSWMN ESVQKSDNYN SYAEVNMVIA GSYNYYFTIN GTLKANGGGY FLVDPILRTG
SMDDRLPLDS ICCQTVMPKL LGPFLEWASR LMVSKESGYN MIHFTPIQEL GKSDSCYCLK
DQRKLDPRYS SKDKTFTMDD VKLLVNTMNE EWGVLSLTDL VFNHTANESP WILEHPECAY
NLINSPHLKP AYLMDRILWH FSMDVGKGLY ESLGVPAKFD SEHYLYNIRR ILEDDILPRY
KFWEFHQCNI EETIAQFKVA ILRDDKPVTD LVLIPNVEYR RLECTVDIPQ AIKNYYSNHN
ISRDIRINVA CDNLRHKLQE LNSASGYSMM EHVHTAVNNF IANAKYRFID PAGLRLSLVG
PDTPLMWNYF TLPTEEMSVE EEEREMNTER GGAYCMAHNG WVMSDDPLRN FAEPGSNVYL
RRELLPWGDS VKLRYGNRME DCPFLWQYMK NYATETASIF HGVRLDNCHS TPIHVAEYML
DEARKVRPDL YVIAELFTNS EYADNTFINR LGINSLIREG LNGLTARELS RLVHRYGGSP
VGSFIQLPAR LIMPSVAHAL FMDQTHDNES VIQKHTAEDL LSYTAIISMT CSATGSNRGY
DEMVPHYIHV VEESRPYKKW LVEGKLNPKT HCNMNSGIVR AKKFFNELHI NLDRSGFKEV
YVDMITDEVM SITRHNPVSH QSVILYAHTC FRANDRGGSL HNITIPGVVD EIIIEGFLQK
DREEEFVKQD DHINGLNNYK LSLSENIQAT HSKILKIIDP ENTNSNTIHF HNLVPGAIAV
LKVLPPEEVR PAFMKTRQIL SGFGYQMKTL SSRKVSLTAS PLEVILQEMS LNDLNRVLFR
SDAEERDDGK GFGAYDIPRF GRLTYCGLQG LSFLLDKIRP SNDLGHPLCD NLRQGDWLMD
YIANRLLAHQ GTAQLGKWFE NTFAALKKVP RYLIPSYFDA VVNGVCTMAV DACWDKMSTF
TSDGSKFVRD LSLGSVQMCS YVRSAKLPKL SSSLSKPHPP KHVDFDGSTV EACTTLCAGL
PHFSTGLFRN WGRDTFISLR GNLIITGRYV EARFIILGYA GCLRHGLIPN LLGEGISARY
NCRDAVWFWL QCIKDFCSLA PNGSSILKDR VMRLYPSDDA PVTVHVDQTL EEVMQEALQR
HATGIRFRER HAGNQIDSEM KHEGFNVDAG IDWRTGFVYG GNDFNCGTWM DKMGSSWKAG
NKGVPATPRD GSAVELIGLS ASVVHWLSSM HANHLYPYPH VVGCSQTHTW SQWYDLIRSY
FEKYFWIDPM KTLDPTIHDI QLVNRKSIYK DSLGSSRKYT DYQLRCNFPI AIVVCPDLFE
VHHAWQALNM LEKYLVGPLG VKTLDPSDYN YVGDYYNGDD SDDYKRSRGF NYHQGPEWIW
PMGYFLRAKL IIAQRLSASK ENANILNETM TYVEKVMTSH NVHLQQSPWK SLPELTNSDG
KHCADSCEAQ AWSVGCLLEV LHEMALIRNQ
//
