ID   GDE_YEAST               Reviewed;        1536 AA.
AC   Q06625; O93808;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 67.
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 (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
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   MEDLINE=20334447; 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
RT   and its competent purification method.";
RL   Protein Expr. Purif. 19:298-303(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; 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.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   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.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
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
RT   debranching enzyme.";
RL   FEMS Microbiol. Lett. 193:105-110(2000).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, AND MASS
RP   SPECTROMETRY.
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).
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-
CC       glucosidase in glycogen degradation.
CC   -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan
CC       to a new position in an acceptor, which may be glucose or a
CC       (1->4)-alpha-D-glucan.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->6)-alpha-D-glucosidic branch
CC       linkages in glycogen phosphorylase limit dextrin.
CC   -!- INTERACTION:
CC       P43598:-; NbExp=1; IntAct=EBI-37861, EBI-22956;
CC       P27472:GSY2; NbExp=1; IntAct=EBI-37861, EBI-8036;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the glycogen debranching enzyme family.
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DR   EMBL; AB018078; BAA34996.1; -; Genomic_DNA.
DR   EMBL; U25842; AAB68117.1; -; Genomic_DNA.
DR   PIR; S59841; S59841.
DR   RefSeq; NP_015510.1; -.
DR   DIP; DIP:2578N; -.
DR   IntAct; Q06625; 23.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PeptideAtlas; Q06625; -.
DR   PRIDE; Q06625; -.
DR   Ensembl; YPR184W; Saccharomyces cerevisiae.
DR   GeneID; 856314; -.
DR   GenomeReviews; U00094_GR; YPR184W.
DR   KEGG; sce:YPR184W; -.
DR   NMPDR; fig|4932.3.peg.6659; -.
DR   CYGD; YPR184w; -.
DR   SGD; S000006388; GDB1.
DR   HOGENOM; Q06625; -.
DR   OMA; Q06625; AHALFMD.
DR   BioCyc; MetaCyc:MON-13683; -.
DR   BRENDA; 2.4.1.25; 250.
DR   BRENDA; 3.2.1.33; 250.
DR   NextBio; 981694; -.
DR   ArrayExpress; Q06625; -.
DR   GermOnline; YPR184W; Saccharomyces cerevisiae.
DR   GO; GO:0005739; C:mitochondrion; IDA: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:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0005980; P:glycogen catabolic process; IMP:SGD.
DR   InterPro; IPR010401; GDE_C.
DR   InterPro; IPR006421; Glyc_debranch.
DR   InterPro; IPR013781; Glyco_hydro_sg_catalytic.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   PANTHER; PTHR10569; GDE_C; 1.
DR   Pfam; PF06202; GDE_C; 1.
DR   TIGRFAMs; TIGR01531; glyc_debranch; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Glycogen biosynthesis; Glycosidase; Glycosyltransferase; Hydrolase;
KW   Mitochondrion; Multifunctional enzyme; Phosphoprotein; Transferase.
FT   CHAIN         1   1536       Glycogen debranching enzyme.
FT                                /FTId=PRO_0000087452.
FT   REGION        1      ?       4-alpha-glucanotransferase.
FT   REGION        ?   1536       Amylo-1,6-glucosidase.
FT   ACT_SITE    535    535       By similarity.
FT   ACT_SITE    538    538       By similarity.
FT   ACT_SITE    670    670       By similarity.
FT   MOD_RES      45     45       Phosphothreonine.
FT   CONFLICT    368    368       R -> K (in Ref. 1; BAA34996).
FT   CONFLICT    536    536       N -> Y (in Ref. 1; BAA34996).
FT   CONFLICT    774    774       D -> N (in Ref. 1; BAA34996).
FT   CONFLICT   1180   1180       R -> K (in Ref. 1; BAA34996).
FT   CONFLICT   1289   1289       K -> N (in Ref. 1; BAA34996).
FT   CONFLICT   1489   1489       F -> S (in Ref. 1; BAA34996).
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
//