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Database: UniProt
Entry: A0A0Q9X9A0_DROMO
LinkDB: A0A0Q9X9A0_DROMO
Original site: A0A0Q9X9A0_DROMO 
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
//
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