ID A0A0Q9X9A0_DROMO Unreviewed; 1538 AA.
AC A0A0Q9X9A0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=Dmoj\GI19003 {ECO:0000313|EMBL:KRG04693.1};
GN ORFNames=Dmoj_GI19003 {ECO:0000313|EMBL:KRG04693.1};
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230 {ECO:0000313|EMBL:KRG04693.1, ECO:0000313|Proteomes:UP000009192};
RN [1] {ECO:0000313|EMBL:KRG04693.1, ECO:0000313|Proteomes:UP000009192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG04693.1}, and Tucson
RC 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [2] {ECO:0000313|EMBL:KRG04693.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG04693.1};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:KRG04693.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#15081-1352.22 {ECO:0000313|EMBL:KRG04693.1};
RG FlyBase;
RL Submitted (NOV-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}.
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DR EMBL; CH933808; KRG04692.1; -; Genomic_DNA.
DR EMBL; CH933808; KRG04693.1; -; Genomic_DNA.
DR EMBL; CH933808; KRG04695.1; -; Genomic_DNA.
DR RefSeq; XP_015019296.1; XM_015163810.1.
DR RefSeq; XP_015019297.1; XM_015163811.1.
DR RefSeq; XP_015019299.1; XM_015163813.1.
DR EnsemblMetazoa; FBtr0425024; FBpp0382817; FBgn0141742.
DR EnsemblMetazoa; FBtr0427445; FBpp0385063; FBgn0141742.
DR EnsemblMetazoa; FBtr0428269; FBpp0385829; FBgn0141742.
DR GeneID; 6579677; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000009192; 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, ECO:0000313|EMBL:KRG04693.1};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KRG04693.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KRG04693.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRG04693.1}.
FT DOMAIN 31..133
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 141..582
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 720..990
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1058..1526
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1538 AA; 173305 MW; D171A2E13B36DE58 CRC64;
MSKDTDSHSI PITEGTNAEH VLYRLKRGSK LRVHPDVALL GRKILLHTNY PAEGKKFVRT
EYRVLGWQLK DGQQITSDAH PDVHVVDTDI FSELTLNMSG TFRFYFSFAD VERKADSPPD
GALYVQVEPT LHVGPVGAQK IIPLNSVRCQ TVMAKLLGPL NTWEAKLRVA KESGYNVIHF
TPIQELGGSR SGYSLRDQLC VNSQFAAKKG EKVTFEDVEK IIKKCRQEWG VASICDIVLN
HTANESEWLI KHPDATYSCA TCPYLRPAFL LDAMLAQCGA DIAAGSLEHV GVPAIIDQEC
HLEALKYQLH NVYLPKVNIH ELYQCDVMKY VTEFMAQVRT REPPKNVANK SRFQEIQLIQ
DSAYRRLGST INIELALEIF NAFHGDCFDE ESRFRKCAET LRHHLDELNE RVRAELQGYL
TYAIDNCLAG VRYERVQHDG PRVREISIKH SVFMTYFTHT NTEGKTLTEV EADMYGKAGE
FFMAHNGWVM GSSDPLLDFA EEQPGRGNVY LKRELISWGD SVKLRFGKRP EDSPYLWKHM
TDYVETTARI FDGVRLDNCH STPLHVAEYL LDAARKINPE LYVVAELFTN SDATDNVFVN
RLGITSLIRE ALSAWDSHEQ GRLVYRYGGA PVGGFYANPN RDVAPSVAHA LFMDLTHDNP
SPVEKRSVYD LLPSSALVAM ACCATGSNRG YDELVPHHIH VVDEERPYQE WGKAVDFKTG
IIAAKRALNL LHGQLAEEGF SQVYVDQMDP NVVAVTRHSP ITHQTVILVA HTAFSYPHPN
AGPTNVRPLR FEGVLDEIIL EANLTLKSDK PFDRPAPFKK ADNVLNGFTQ FELSLQEHIP
LSKSQVFETN QYTDGSNTQL NFANLRPGTV VAIRVSMRPD ARLSFDRLQQ VTNALRLVSG
EQCEELKAIV SKLDLTALSR ALFSCDQEER DMGLGCSAYD IPNFGPIVYC GLQGFVSLLT
EISPRDDLGH PLCNNLRDGN WMMDYIADRL NNFNDLKPLS TWFKATFEPL KNVPRYLIPC
YFDAIVSGVY NILVNQVNQL MPSFIRDGHN FTQSLAVSTL QFLAVCNSAN LPGFSLALAP
PKPPKQCVTL SAGLPHFSTG YMRCWGRDTF IALRGTMLLT GRFTEARFII IGFASAMRHG
LIPNLLDNGV KPRFNCRDAV WWWLYSIAQY VEEAPQGANI LKDQVSRIFP YDDSEPHPPG
AFDQLLQDVM QEALQVHFQG LQYRERNAGH EIDAHMTDQG FNNHIGVHPE TGFVFGGNSA
NCGTWMDKMG SSEKAGNRGR PSTPRDGSAV ELIGLQYASL RFMQSLSERK IIPHSGVERK
GPSGEVTKWS YKEWADRIQK NFDAYFYVKE TDTTSVANKK CIYKDSYGAT QDWTDFQLRC
NFPITLTVAP ELCNPKNAWK ALEQARKHLL GPLGMKTLDP DDWNYRANYD NSNDSTDCTV
AHGANYHQGP EWVWPIGFYL RARLIFAKKC GYLDETIAET WAILRAHLRE IQTSHWRGLP
ELTNDNGSYC RDSCRTQAWS VGTVLEVLHD LHSLGADC
//