ID   GDE_YEAST               Reviewed;        1536 AA.
AC   Q06625; D6W4I4; O93808;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Glycogen debranching enzyme;
DE   AltName: Full=Glycogen debrancher;
DE   Includes:
DE     RecName: Full=4-alpha-glucanotransferase;
DE              EC=2.4.1.25;
DE     AltName: Full=Oligo-1,4-1,4-glucantransferase;
DE   Includes:
DE     RecName: Full=Amylo-alpha-1,6-glucosidase;
DE              Short=Amylo-1,6-glucosidase;
DE              EC=3.2.1.33;
DE     AltName: Full=Dextrin 6-alpha-D-glucosidase;
GN   Name=GDB1; OrderedLocusNames=YPR184W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 208-216;
RP   302-311; 351-358; 1296-1305 AND 1356-1365.
RC   STRAIN=ATCC 56960 / D-346;
RX   PubMed=10873545; DOI=10.1006/prep.2000.1252;
RA   Nakayama A., Yamamoto K., Tabata S.;
RT   "High expression of glycogen-debranching enzyme in Escherichia coli and its
RT   competent purification method.";
RL   Protein Expr. Purif. 19:298-303(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION.
RX   PubMed=11094287; DOI=10.1111/j.1574-6968.2000.tb09410.x;
RA   Teste M.A., Enjalbert B., Parrou J.L., Francois J.M.;
RT   "The Saccharomyces cerevisiae YPR184w gene encodes the glycogen debranching
RT   enzyme.";
RL   FEMS Microbiol. Lett. 193:105-110(2000).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA   Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA   van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT   "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT   phosphorylation in assembly of the ATP synthase.";
RL   Mol. Cell. Proteomics 6:1896-1906(2007).
RN   [8]
RP   INTERACTION WITH IGD1, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=21585652; DOI=10.1111/j.1567-1364.2011.00740.x;
RA   Walkey C.J., Luo Z., Borchers C.H., Measday V., van Vuuren H.J.;
RT   "The Saccharomyces cerevisiae fermentation stress response protein
RT   Igd1p/Yfr017p regulates glycogen levels by inhibiting the glycogen
RT   debranching enzyme.";
RL   FEMS Yeast Res. 11:499-508(2011).
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:0000269|PubMed:11094287,
CC       ECO:0000269|PubMed:21585652}.
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;
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   -!- ACTIVITY REGULATION: Activity is inhibited by IGD1.
CC       {ECO:0000269|PubMed:21585652}.
CC   -!- SUBUNIT: Interacts with IGD1. {ECO:0000269|PubMed:21585652}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC       Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB018078; BAA34996.1; -; Genomic_DNA.
DR   EMBL; U25842; AAB68117.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11600.1; -; Genomic_DNA.
DR   PIR; S59841; S59841.
DR   RefSeq; NP_015510.1; NM_001184281.1.
DR   AlphaFoldDB; Q06625; -.
DR   SMR; Q06625; -.
DR   BioGRID; 36356; 44.
DR   DIP; DIP-2578N; -.
DR   IntAct; Q06625; 7.
DR   MINT; Q06625; -.
DR   STRING; 4932.YPR184W; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   CAZy; GH133; Glycoside Hydrolase Family 133.
DR   iPTMnet; Q06625; -.
DR   MaxQB; Q06625; -.
DR   PaxDb; 4932-YPR184W; -.
DR   PeptideAtlas; Q06625; -.
DR   TopDownProteomics; Q06625; -.
DR   EnsemblFungi; YPR184W_mRNA; YPR184W; YPR184W.
DR   GeneID; 856314; -.
DR   KEGG; sce:YPR184W; -.
DR   AGR; SGD:S000006388; -.
DR   SGD; S000006388; GDB1.
DR   VEuPathDB; FungiDB:YPR184W; -.
DR   eggNOG; KOG3625; Eukaryota.
DR   GeneTree; ENSGT00390000012596; -.
DR   HOGENOM; CLU_001517_2_0_1; -.
DR   InParanoid; Q06625; -.
DR   OMA; YEEGHVH; -.
DR   OrthoDB; 1427975at2759; -.
DR   BioCyc; MetaCyc:YPR184W-MONOMER; -.
DR   BioCyc; YEAST:YPR184W-MONOMER; -.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis).
DR   BioGRID-ORCS; 856314; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q06625; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q06625; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0004134; F:4-alpha-glucanotransferase activity; IDA:SGD.
DR   GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IDA:SGD.
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; IMP:SGD.
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; Direct protein sequencing; Glycogen biosynthesis; Glycosidase;
KW   Glycosyltransferase; Hydrolase; Mitochondrion; Multifunctional enzyme;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1536
FT                   /note="Glycogen debranching enzyme"
FT                   /id="PRO_0000087452"
FT   REGION          1..?
FT                   /note="4-alpha-glucanotransferase"
FT   REGION          ?..1536
FT                   /note="Amylo-1,6-glucosidase"
FT   ACT_SITE        535
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        538
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        670
FT                   /evidence="ECO:0000250"
FT   CONFLICT        368
FT                   /note="R -> K (in Ref. 1; BAA34996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        536
FT                   /note="N -> Y (in Ref. 1; BAA34996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        774
FT                   /note="D -> N (in Ref. 1; BAA34996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1180
FT                   /note="R -> K (in Ref. 1; BAA34996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1289
FT                   /note="K -> N (in Ref. 1; BAA34996)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1489
FT                   /note="F -> S (in Ref. 1; BAA34996)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1536 AA;  174972 MW;  167270B2EE15EDF9 CRC64;
     MNRSLLLRLS DTGEPITSCS YGKGVLTLPP IPLPKDAPKD QPLYTVKLLV SAGSPVARDG
     LVWTNCPPDH NTPFKRDKFY KKIIHSSFHE DDCIDLNVYA PGSYCFYLSF RNDNEKLETT
     RKYYFVALPM LYINDQFLPL NSIALQSVVS KWLGSDWEPI LSKIAAKNYN MVHFTPLQER
     GESNSPYSIY DQLQFDQEHF KSPEDVKNLV EHIHRDLNML SLTDIVFNHT ANNSPWLVEH
     PEAGYNHITA PHLISAIELD QELLNFSRNL KSWGYPTELK NIEDLFKIMD GIKVHVLGSL
     KLWEYYAVNV QTALRDIKAH WNDESNESYS FPENIKDISS DFVKLASFVK DNVTEPNFGT
     LGERNSNRIN VPKFIQLLKL INDGGSDDSE SSLATAQNIL NEVNLPLYRE YDDDVSEILE
     QLFNRIKYLR LDDGGPKQGP VTVDVPLTEP YFTRFKGKDG TDYALANNGW IWNGNPLVDF
     ASQNSRAYLR REVIVWGDCV KLRYGKSPED SPYLWERMSK YIEMNAKIFD GFRIDNCHST
     PIHVGEYFLD LARKYNPNLY VVAELFSGSE TLDCLFVERL GISSLIREAM QAWSEEELSR
     LVHKHGGRPI GSYKFVPMDD FSYPADINLN EEHCFNDSND NSIRCVSEIM IPKILTATPP
     HALFMDCTHD NETPFEKRTV EDTLPNAALV ALCSSAIGSV YGYDEIFPHL LNLVTEKRHY
     DISTPTGSPS IGITKVKATL NSIRTSIGEK AYDIEDSEMH VHHQGQYITF HRMDVKSGKG
     WYLIARMKFS DNDDPNETLP PVVLNQSTCS LRFSYALERV GDEIPNDDKF IKGIPTKLKE
     LEGFDISYDD SKKISTIKLP NEFPQGSIAI FETQQNGVDE SLDHFIRSGA LKATSSLTLE
     SINSVLYRSE PEEYDVSAGE GGAYIIPNFG KPVYCGLQGW VSVLRKIVFY NDLAHPLSAN
     LRNGHWALDY TISRLNYYSD EAGINEVQNW LRSRFDRVKK LPSYLVPSYF ALIIGILYGC
     CRLKAIQLMS RNIGKSTLFV QSLSMTSIQM VSRMKSTSIL PGENVPSMAA GLPHFSVNYM
     RCWGRDVFIS LRGMLLTTGR FDEAKAHILA FAKTLKHGLI PNLLDAGRNP RYNARDAAWF
     FLQAVQDYVY IVPDGEKILQ EQVTRRFPLD DTYIPVDDPR AFSYSSTLEE IIYEILSRHA
     KGIKFREANA GPNLDRVMTD KGFNVEIHVD WSTGLIHGGS QYNCGTWMDK MGESEKAGSV
     GIPGTPRDGA AIEINGLLKS ALRFVIELKN KGLFKFSDVE TQDGGRIDFT EWNQLLQDNF
     EKRYYVPEDP SQDADYDVSA KLGVNRRGIY RDLYKSGKPY EDYQLRPNFA IAMTVAPELF
     VPEHAIKAIT IADEVLRGPV GMRTLDPSDY NYRPYYNNGE DSDDFATSKG RNYHQGPEWV
     WLYGYFLRAF HHFHFKTSPR CQNAAKEKPS SYLYQQLYYR LKGHRKWIFE SVWAGLTELT
     NKDGEVCNDS SPTQAWSSAC LLDLFYDLWD AYEDDS
//