ID A0A0V1CT18_TRIBR Unreviewed; 1742 AA.
AC A0A0V1CT18;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:KRY52326.1};
GN ORFNames=T03_16641 {ECO:0000313|EMBL:KRY52326.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52326.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52326.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52326.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- SIMILARITY: Belongs to the nematode transthyretin-like family.
CC {ECO:0000256|ARBA:ARBA00010112}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY52326.1}.
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DR EMBL; JYDI01000107; KRY52326.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CT18; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.60.40.3330; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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; IPR032792; AGL_glucanoTrfase.
DR InterPro; IPR032790; GDE_C.
DR InterPro; IPR006421; Glycogen_debranch_met.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR001534; Transthyretin-like.
DR InterPro; IPR038479; Transthyretin-like_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; PF01060; TTR-52; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1606..1625
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 145..583
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 734..1028
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1123..1581
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY52326.1"
SQ SEQUENCE 1742 AA; 198413 MW; D8C363C2564270FF CRC64;
LLHCLPVSCV MISTSFFLFS MDNLTYTLTL EYGLNTESKL YQVQKGSTIR FVTGSSLFGM
DVYFSTTYPE SELNINRYEA VWRQLEWNQG SDNSADDFGR YIDIKCDIAG PHMFSFCYNP
GDVSLHDGIG YFLVLPTLTV GKSKKEIPLH AIQCQTVLAK LLGPFDEWEQ RLRVSKESGY
NMVHITPIQE LGQSNSSYSI ADQLTLNPIF KGKGEEYTLL DVKKLVQKMN EDWEMLVISD
VVWNHTASNS SWLRTEPDCA YNMKNSPHLR PAWLLDRVLA HFGRLIANGK FEASGLPSKS
RWDNENLENL RHMLLNDILP PARFHEFFQV NIDKEVQQFA DEIAELNKPS SVVLQTEQCL
RILQDPSYRR LNCTLDSHAL ALLLFNRAVD GCSDEKERQR ICVENFRRAV KELNDNAARD
CWNHLHVAVN ALIGHVSYQR VQDHGPKFMD FTEHHPLFPQ YFLYPGKWEA SWEDEENMMY
TQEGTRFMAL NGWVMDDIPL TNFAEPPSMV YFRRELVCWG DSVKLRYGMS EADNPYLWRR
MSSYTRKTAE IFHGIRIDNC HNTPIHVAEY MLNEARDARP ELYVCAELFT SREDVDNLFV
NRLGIVSLIR EAMSAPTPDE LGRLVHRYGG EPIGSFMPYP YRPLASSVAQ AFFFDLTHDN
CSPIMSKSVY DVLPTAAIVS SACCAIGSNR GLDELIPYHI HVVSEKRLYC SWATEDESTA
KKAVADGTVC METGILKARL ALNKLHLYLS THGFTQLYVD RKTDEVHVIK RQNPITCESV
VIVARNCFNP AGTASRCALL APCSLIGDLK TILLEANVEI GELPPDCRSH PIGPRSSTES
CPPLSDGEQF LTGLKNVHLK MFENLKVFNS SMIERVESIS SQNSEVEFAE LPAGAVLAMM
VTLKPEAREA VHTLRYELAL IGFNGYQSIP PEDMNNFQSS VKPLSKILEK LSLVDFSYVL
YRCDEEERSE YPDQGTYFVP DYGKLTFCGL QGCISVLKEA KASNNLGHPI CKNIRDGDWL
ADYIVARLKL NPNTVQLSEW FWEIFAIYKK IPFDLKPSYF EAIISSVYSM VCKTIVQKMS
LFIGRGSDFL KNLAISSLMF CNHCKDALLP EVSHMVEFTD NCHQYSYPYQ KIMPSIAAGL
PHFSHGLFRN WGRDTFIALP GILLITGRYD EAKYIILAYG SCLRHGLIPN LVGEGNFARY
NCRDAVWWWL LAIRCYCELK KDFSILTQPV RRLFPSTDTG FSTVPIEQPL RETMQEALEA
HFYGTNFREE NAGPQIDEHM RDEGFNVEIG VDKSTGFVYG GNGWNCGTWM DKMGSSDLAI
NRGVPATPRD GSAVELIGLS YAVISWLSSA HQLKAYPFNG VRKRKSSDEV WTWENWKIML
IENFERHFWI PMQDCPDANL VELDLDLVNV RGIYKDSYKA SNRWADYQFR PNFLITMTLA
PDLFKVGNAL CALKQAEELL LGPLGVKTLT TRDMAYNGNY DNSDSSADYR RANGFNYHNG
PEWVWIFGYF LRAKMTFAYL KNKQTSGVLD EAMSSVKKLL GPHWEHLQKS PWFSLPELTN
ANGSFCRDSC EAQAWSIGSL LQCRRRCRKS GLFLELHCLT LARMKLFLFF FTVFGILYSS
CALLGRMQRV AAKGKLFCGA KPAAGVKVKL IDIDTGFDDV MDEKRTNANG EFYVDGQTSE
ITDIDPVLKI YHDCHDGKPC QRRWKVEIPK RYIASPNKQP NVFELGTINL EAYWHDEERN
CV
//
