ID A0A0N5CB21_STREA Unreviewed; 1476 AA.
AC A0A0N5CB21;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 22.
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 Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001508500.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001508500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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; 174720.A0A0N5CB21; -.
DR WBParaSite; SPAL_0001508500.1; SPAL_0001508500.1; SPAL_0001508500.
DR Proteomes; UP000046392; Unplaced.
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; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 114..533
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 670..923
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 992..1459
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1476 AA; 169334 MW; 7E6B80157D2A4B96 CRC64;
MTLKNKGHRE IRIVVLEKNY DGKHIFLQLK RGWFVRFQLG ETLVTNNVNI TIYRNGEKEF
ENQLKSGKFG KDSFLDIECK VAGSYYYEYE SDNDINGKGY YHVEPELIVK DDQKIPLDAI
SCQTYLTKLL GHFSEWKDKL KVARELGYNM IHLTPIQTLG ISDSCYSISN HLTLDSRYKG
DLHDVEKLIQ KMRDKWGMLV IQDVVWNHAA KNAKWLKEHP ECTFNCINSP HLRPAYLLDR
ALLYFSEEIR DGKWEDKGIP TIIDSPSHLN AIRHALQHTI IPNLRLWEFF QVDIESVIQI
CLREAGIMEV YGGVSIDSIN NEDISIIQDP EYKRFSCTIN YDSGIKLALQ KGQNGLMEKL
RILNHDMFLK INDMMMEAIN AIIGHINYER ISDDGPKLGK VSDDHPLLTN YFAYPTGSST
IEEDEEIIFD KIKGQQCRAC NGWVMGDDPL KNFAESHSQV YLKRQLISWG DSLKLNYGME
PGHCPYLWKY MKEYTETCAR IFSGFRIDNC HSTPIHVAEY LLNAARKIKP NLYVVAELFT
GSEEIDNIFV NRLGITSLIR EAQNCQNKEQ GRMVYRYGGK QMASFMGQEC KALNSVAHAL
LYDQTHDNPS PVNKFGSMYC YLPTASLVST TACAIGSTRG FDEFVTFTID VVKEKRLYKN
WSEVQEDNYG LIKARKLIND LHSKMAYEGY TEVFADQVTD TVVAVTRRNP TNNEVIIIIT
HNCFGQFEWN PQAKDIVVCG KVNKIIFEMK TIENTETEDR KIPEDKINGV SKFIVDIKED
LKPSESHSLE IVHENVIKFK NFPSGSVVAL QIIQDESSMS AINDIETFIN DEHSPRLEKI
KKAIGELDLY YFNKLLFRVD GEEREDSNDH TYNIPHWGSL PYCGLQGVRN LLKRVASDND
QGHPLCHNIR NGNWLAEYCY KRLQRGKELK KIGDAFQDVL GVLENIPSNV RPAYFERVFN
ILYKEVRKGF LKKLRANIDL PTCNLVTRLL LSSASFVSYV KNAELSPISE KLFTTEQYPS
SLAAGLPHFT TGIWRNWGRD TFIALPGILL LSGRFVEARN IIISYAGTLR HGLIPNLLAA
GKGARYNCRD AVWFWLAAIM KYIEMAPCGP EILERPVIRV YKNDDAEFDS NGHEQPLKDV
ILEALSRHFN GIEFRERNSG RDIDEHMQNE GFNVHAFVHP GTGFICGGNQ YNCGTWMDKM
GSSTIAGNKG YPATPRDGAA VEIQGLAVYV LESLEKLYEK GLYSTNRVTN TKNGMSWTFK
EWAGKIRTYF PNFFYVHENE SDEMAHRRGI IKDCFGSTAR YTDFQLRPNF TIALCHAPDI
IETNKAWSSL KMAEKVLMSR LGIKTLDPQD WAYCGNYNNQ DSQDKKTACG WNYHQGPEWL
WVACCYLKAK LEIGWRRKLE GHKKDWIDVC KEITKQLYIY EEYIDNSLWA SLPELTNENG
AHCPPSCEAQ AWSIGCLLEV VHRYNQLLKM DEKLEL
//
