ID I1RZ78_GIBZE Unreviewed; 1553 AA.
AC I1RZ78; A0A098DP59;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 66.
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=FG09704.1 {ECO:0000313|EnsemblFungi:CEF83646};
GN ORFNames=FGRAMPH1_01T26479 {ECO:0000313|EMBL:CEF83646.1};
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533 {ECO:0000313|EMBL:CEF83646.1, ECO:0000313|Proteomes:UP000070720};
RN [1] {ECO:0000313|EnsemblFungi:CEF83646, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF83646};
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2] {ECO:0000313|EnsemblFungi:CEF83646, ECO:0000313|Proteomes:UP000070720}
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1 / ATCC MYA-4620 / FGSC
RC 9075 / NRRL 31084 {ECO:0000313|EnsemblFungi:CEF83646};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3] {ECO:0000313|EMBL:CEF83646.1, ECO:0000313|Proteomes:UP000070720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1
RC {ECO:0000313|Proteomes:UP000070720}, and PH-1
RC {ECO:0000313|EMBL:CEF83646.1};
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4] {ECO:0000313|EnsemblFungi:CEF83646}
RP IDENTIFICATION.
RC STRAIN=PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084
RC {ECO:0000313|EnsemblFungi:CEF83646};
RG EnsemblFungi;
RL Submitted (JAN-2017) to UniProtKB.
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; HG970335; CEF83646.1; -; Genomic_DNA.
DR RefSeq; XP_011328001.1; XM_011329699.1.
DR STRING; 229533.I1RZ78; -.
DR EnsemblFungi; CEF83646; CEF83646; FGRRES_09704.
DR GeneID; 23556643; -.
DR KEGG; fgr:FGSG_09704; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G26479; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; I1RZ78; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000070720; Chromosome 4.
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};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000070720};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 42..141
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 145..577
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 752..996
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1079..1540
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
FT REGION 629..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1553 AA; 174951 MW; D13220A2CE00701A CRC64;
MSPPHTMTSN EVYLLPLNDD GSPQVQGEYI YLAPRSQEPI TVRFAIEGTS SICRHGSLWV
NIPDEGAEFR RDHFREFKLT PDFNRTLEIS IPIHQPGAYA FYTTYAELPE LKKELKNSSE
QKENLKKTPL YYIDVAPRLK LDGRPLPLPA LSIFSVISKF MGKYPNDWER HLHGISDRGY
NMIHFTPLQI RGISNSPYSL YDQLGWDPAC FPAGEDDVQK MVESLERNHS LLSLTDIVLN
HTANNTKWLE EHPEAGYNLL TAPWLESAYQ LDTSLLELSD NLAKLGLPTD VKSTDDLMLI
MDAIKTEVLA KIRLWEYYAL DVDRDADEAI KAFSKGSKYS SDDTADFEKK LEKAKSGSVK
EQVDFFREVG LAGTDRMGER FRKRVKPDVA ASFLAGSSDE SAARAKIVEI LNILNVDFYK
EYDAEVDDIL QQIFNRIKYV RLDEHGPKLG EINKENPLIE PYFTRLPKND TTSKLKPEEM
ALVNNGWVWG GNALVDNAGP DSRVYLRREV IVWGDCVKLR YGSGPKDNPW LWEHMTKYAR
TLAKYFAGLR IDNCHSTPIH VAEHILDEAR RVRPDLYVVA ELFTGSEEMD YVFVKRLGLS
SLIREAMQAW STAELSRLVH RHGGRPIGSF EVDEVSKSDV RTPSSSPTRL KNGDTNGNGP
RSREIIRAIK PSPVHALFMD CTHDNETPAQ KRDARDTLPN AALVCMCSSA TGSVMGYDEI
YPKLVDLVNE TRLYTSASSG SKPIKIGGGE DGIGGIKKLL NQIHTLMGKD GYDETHIHHE
DQYITVHRVH PESRKGYFLI AHTAFPGYGN GNGDFSPVHL TGTKARHLGS WMLEVDASEE
ATRQALSDKK YLRGLPSRVK DVPGIRMEVN GDDTTITVRD RFPPGSIALF ETWIPAAEHS
SGLDNYVTSG AKAAWSELSL SDLNFLMYRC EAEERDESDG RDGVYDIPGH GKLVYAGLQG
WWSILKNIIK ENNLAHPLCQ NLRDGEWALD FILARLQRIS ATPGNQAVAE PLKWLQERFE
AIRKIPSFLL PRYFGLVLRT AYMASWERSL QLMNASVRDG QWFLQSLAMV SVQQVGYVKS
ASLWPNKLVP SLAAGLPHFA VEWARCWGRD VFIALRGLLL GTGRFDDAKE HILAFASVLK
HGMIPNLLSS GDAPRYNSRD SIWFFLQCIQ DYTRFAPEGL DILKVKVKRR FLPYDDTWFP
TDDERAYSKE STIEEVIQEA LQRHATGMKY REANAGPQID SQMKDEGFNQ DIHVDWNNGI
IFGGNQDNCG TWMDKMGESE RAGSKGVPGT PRDGAAIEIT GMLYSTLDWL AGLHGKGKYA
YAGVEKSDGS SISLADWASL LKANFERCYY VPISAEDDSK YDVNTPIVNR RGIYKDLYKS
GKEYEDYQLR PNFAIAMTTA PALFDPDHAM HALCVADEAL RGPQGMATLD PADLNYRPYY
VNSEDSDDFA TSKGRNYHQG PEWIWPTGFF LRALLKFDLK RRTTAEDRTE AFQQVTRRLG
GCKKMIQESP WAGLQELTQK NGEYCADSSP TQAWSAGCLI DLYMDAVEEQ NGA
//
