ID A0A182VML3_ANOME Unreviewed; 1532 AA.
AC A0A182VML3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-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};
OS Anopheles merus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=30066 {ECO:0000313|EnsemblMetazoa:AMEM017540-PA, ECO:0000313|Proteomes:UP000075903};
RN [1] {ECO:0000313|Proteomes:UP000075903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAF {ECO:0000313|Proteomes:UP000075903};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles merus MAF (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEM017540-PA}
RP IDENTIFICATION.
RC STRAIN=MAF {ECO:0000313|EnsemblMetazoa:AMEM017540-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; 30066.A0A182VML3; -.
DR EnsemblMetazoa; AMEM017540-RA; AMEM017540-PA; AMEM017540.
DR VEuPathDB; VectorBase:AMEM017540; -.
DR VEuPathDB; VectorBase:AMEM21_010272; -.
DR Proteomes; UP000075903; 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; 1.50.10.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
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; 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 Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 32..132
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 140..578
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 716..984
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1078..1520
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1532 AA; 173198 MW; 608D87E2E943A2EF CRC64;
MADGVISIKL AIHDSNQGDG ALYRLKKNSL VHVHPGASLL GRRVALYCNY PADDKEFCRK
TYRRLEWCSA AGSPLETSAS GSEYTSIKDV DYYCNVHFTK SGAYHFYALY EECPEAGAQA
GLYVQIEPQL SVGSGEAATT LPLDAIRCQT VISKLLGPLD TWEAKLRVGK ESGYNMIHFT
PVQELGGSRS AYSLRNQLKV NPDFQSKGGK EVNYDDLAVL MRKMREEWNV ASICDIVLNH
TANESIWIRE YPECSYNCFT CPHLRPAFLL DAMLARVGED VKDGMLAHVG VPEVVETEDH
LQAIRWQIHS NYLPQVKLYE LYQCDVDKYV SRFNDECSKR SPSRAQDIPE GDIKLRMDPE
HRRLGAEIDF ERAMSIYNVF RQDCFDEDSR KRKCTEVFRA RLQFLNEEVR REIQEHLDYA
IDNCLAGTRY ERVQGDGPQV KGISVKYPLF MKYFTHYGTQ GKSLKDIESM MYGGAGKLFM
AHNGWVMNGD PLKDFARAQP GTGNVYLRRE LIAWGDSVKL RYGDKPEDSP YLWKHMQEYV
DTTARIFDGV RLDNCHSTPL HVAEYLLDSA RKVNPELYVA AELFTNSDHT DNIFVNRLGI
TSLIREALSA WDSHEQGRLV YRYGGAPVGA FFPCPKRILA PGIAHALFMD LTHDNPSPVE
KRSIFDLIPS AGLVSMACCA TGSNRGYDEF VPHHVHVVDE ERQYQEWGKH VDKNTGLIAV
KEAFNVLHGG LASRGFDQLF VDQMHPDIVA VTRHSLSNHE TVILVAHTAF SYPNPWAGPT
GVRPLEFEGE FKEIILEVQI YKKTGQTFDR PTDFAKNVDY INGVNEYVVD LKRNLKLEES
DIFAKEAVVK GNVTQLHFSN LKPGSVVAVR VALKESVRVH FDTLQSLVRE FHQDRGSRYA
ELQHILSKLD LVDFNKLLYC CAEEERDNGG GPYNVEGYGD LVYCGLQGVM SILSEIGPNN
DLGHPLANNL RNGNWLIDYC SQRLMKYEKL VPMAKWLENN LKSLKEIPRY MIPSYFDVII
TNVHRLAMAA ACNLMSDFVR HGSNFARRLA LGSVQCVADC PSASLPKLSP NVSDPKPPSH
CATMAAGLPH FATGYMRCWG RDTFIAIRGL TLLTGRFDET RYMILGFGGC LRHGLIPNLL
DGGQNARFNC RDAVWWWLYT IKQYVEEAPN GKSILKDKVS RLYPTDDSEA KAPGECDQML
YEVIQEALTV HFQGLSYRER NAGTRIDAHM KEKGFNNRIG INPDTGFVFG GNNANCGTWM
DKMGSSDKAG NRGIPSTPRD GSAVELVGLQ MASLRFMQAM AEQKVIPVSS VERTSYNGTK
TVWTYKEWAN KIAANFEKEF YVDESCESNY ANKRGIYKDT VGSEIAWTDY QLRCNFPIAL
LAAPELADPK HAWRALENAK KYLLGPLGMK TLDYEDWGYR GNYDNSIDSD DKTVAHGANY
HNGPEWVWPI GFYLRARLIF AKANGVLKET VAETWKILQT HLNELQRCHW RGLAELTNEN
GAYCKDSCRT QAWSMGCVLE VLYDLEKYEK EL
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