ID Q9W2H8_DROME Unreviewed; 1629 AA.
AC Q9W2H8;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 3.
DT 27-MAR-2024, entry version 173.
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=BEST:GH22856 {ECO:0000313|EMBL:AAM70868.2};
GN Synonyms=Dmel\CG9485 {ECO:0000313|EMBL:AAM70868.2};
GN ORFNames=CG9485 {ECO:0000313|EMBL:AAM70868.2,
GN ECO:0000313|FlyBase:FBgn0034618}, Dmel_CG9485
GN {ECO:0000313|EMBL:AAM70868.2};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803};
RN [1] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537568;
RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT euchromatic genome sequence.";
RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN [3] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537573;
RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA Celniker S.E.;
RT "The transposable elements of the Drosophila melanogaster euchromatin: a
RT genomics perspective.";
RL Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN [5] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=12537574;
RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA Karpen G.H.;
RT "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN [6] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA Ashburner M., Anxolabehere D.;
RT "Combined evidence annotation of transposable elements in genome
RT sequences.";
RL PLoS Comput. Biol. 1:166-175(2005).
RN [7] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569856; DOI=10.1126/science.1139815;
RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL Science 316:1586-1591(2007).
RN [8] {ECO:0000313|EMBL:AAM70868.2, ECO:0000313|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX PubMed=17569867; DOI=10.1126/science.1139816;
RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA Dimitri P., Karpen G.H., Celniker S.E.;
RT "Sequence finishing and mapping of Drosophila melanogaster
RT heterochromatin.";
RL Science 316:1625-1628(2007).
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; AE013599; AAM70868.2; -; Genomic_DNA.
DR RefSeq; NP_726062.2; NM_166444.2.
DR AlphaFoldDB; Q9W2H8; -.
DR SMR; Q9W2H8; -.
DR STRING; 7227.FBpp0071526; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR CAZy; GH133; Glycoside Hydrolase Family 133.
DR PaxDb; 7227-FBpp0071526; -.
DR DNASU; 37435; -.
DR EnsemblMetazoa; FBtr0071600; FBpp0071526; FBgn0034618.
DR GeneID; 37435; -.
DR UCSC; CG9485-RB; d. melanogaster.
DR AGR; FB:FBgn0034618; -.
DR FlyBase; FBgn0034618; CG9485.
DR VEuPathDB; VectorBase:FBgn0034618; -.
DR eggNOG; KOG3625; Eukaryota.
DR GeneTree; ENSGT00390000012596; -.
DR InParanoid; Q9W2H8; -.
DR OMA; YEEGHVH; -.
DR OrthoDB; 1427975at2759; -.
DR PhylomeDB; Q9W2H8; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-70221; Glycogen breakdown (glycogenolysis).
DR BioGRID-ORCS; 37435; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37435; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034618; Expressed in capitellum (Drosophila) and 36 other cell types or tissues.
DR ExpressionAtlas; Q9W2H8; baseline and differential.
DR Genevisible; Q9W2H8; DM.
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; 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 1: Evidence at protein level;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:AAM70868.2};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:AAM70868.2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAM70868.2};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q9W2H8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAM70868.2}.
FT DOMAIN 123..223
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 230..672
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 810..1080
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1148..1616
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1629 AA; 183219 MW; 06020245A3AF4929 CRC64;
MRYQLFRWLY GLIATVDNEP LPLQIKSEEE AFGENKKKKQ LASLENAISP GKLDSVAIRT
VPSANANAMG NAGSAEIVSN QIIRRREMST MGKETESHSI PISEGQDAEH ILYRLKRGSK
LSVHPDASLL GRKIVLYTNY PAEGQKFVRT EYRVLGWQLS NGKQITSVMH PEAHVVDTDI
RSQVELNMSG TYHFYFRYLE RPDTGCSGAD GALYVQVEPT LHVGPPGAQK TIPLDSVRCQ
TVLAKLLGPL DTWEPKLRVA KEAGYNVIHF TPIQELGGSR SCYSLRDQLK VNSHFAPQKG
GKISFEDVEK VIKKCRQEWG VASICDIVLN HTANESDWLL QHPDATYSCA TCPYLRPAFL
LDATFAQCGA DIAEGSLEHV GVPAVIEQEC HLEALKYQLH TSYMSKVNIH ELYQCDVMKY
VNEFMSQVRT REPPKNVANE CRFQEIQLIQ DPQYRRLAST INFELALEIF NAFHGDCFDE
ESRFRKCAET LRRHLDALND RVRCEVQGYI NYAIDNVLAG VRYERVQGDG PRVKEISEKH
SVFMVYFTHT GTQGKSLTEI EADMYTKAGE FFMAHNGWVM GYSDPLRDFA EEQPGRANVY
LKRELISWGD SVKLRFGRRP EDSPYLWQHM TEYVQTTARI FDGVRLDNCH STPLHVAEYL
LDAARKINPE LYVVAELFTN SDYTDNVFVN RLGITSLIRE ALSAWDSHEQ GRLVYRYGGV
PVGGFQANSS RHEATSVAHA LFLDLTHDNP SPVEKRSVYD LLPSAALVSM ACCATGSNRG
YDELVPHHIH VVDEERTYQE WGKGVDSKSG IMGAKRALNL LHGQLAEEGF SQVYVDQMDP
NVVAVTRHSP ITHQSVILVA HTAFGYPSPN AGPTGIRPLR FEGVLDEIIL EASLTMQSDK
PFDRPAPFKK DPNVINGFTQ FQLNLQEHIP LAKSTVFQTQ AYSDGNNTEL NFANLRPGTV
VAIRVSMHPG PRTSFDKLQK ISAALRIGSG EEYSQLQAIV SKLDLVALSG ALFSCDDEER
DLGKGGTAYD IPNFGKIVYC GLQGFISLLT EISPKNDLGH PLCNNLRDGN WMMDYISDRL
TSYEDLKPLS AWFKATFEPL KNIPRYLIPC YFDAIVSGVY NVLINQVNEL MPDFIKNGHS
FPQSLALSTL QFLSVCKSAN LPGFSPALSP PKPPKQCVTL SAGLPHFSTG YMRCWGRDTF
IALRGSMFLT GRYNEARFII IGFGQTLRHG LIPNLLDSGS KPRFNCRDAI WWWMYCIKQY
VEDAPKGAEI LKDKVSRIFP YDDADAHAPG AFDQLLFDVM QEALQVHFQG LQYRERNAGY
EIDAHMVDQG FNNQIGIHPE TGFVFGGNNF NCGTWMDKMG SSQKAGNKGR PSTPRDGSAV
ELVGLQYAVL RFMQSLAEKE VIPYTGVERK GPSGEVTKWS YKEWADRIKN NFDKYFFVSE
SETCSVANKK LIYKDSYGAT QSWTDYQLRC NFPITLTVAP DLCNPQNAWR ALERAKKYLL
GPLGMKTMDP EDWNYRANYD NSNDSTDCTV AHGANYHQGP EWVWPIGFYL RARLIFAKKC
GHLDETIAET WAILRAHLRE LQTSHWRGLP ELTNDNGSYC GDSCRTQAWS VAAILEVLYD
LHSLGADVA
//
