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Database: UniProt
Entry: A0A182VML3_ANOME
LinkDB: A0A182VML3_ANOME
Original site: A0A182VML3_ANOME 
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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