GDE_YEAST
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 03-AUG-2022, entry version 173.
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; 37.
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; Q06625; -.
DR PRIDE; Q06625; -.
DR TopDownProteomics; Q06625; -.
DR EnsemblFungi; YPR184W_mRNA; YPR184W; YPR184W.
DR GeneID; 856314; -.
DR KEGG; sce:YPR184W; -.
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; DKMGEST; -.
DR BioCyc; MetaCyc:YPR184W-MON; -.
DR BioCyc; YEAST:YPR184W-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis).
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 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 PANTHER; PTHR10569; PTHR10569; 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; SSF48208; SSF48208; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR TIGRFAMs; TIGR01531; glyc_debranch; 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
