ID N4UG34_FUSC1 Unreviewed; 1556 AA.
AC N4UG34;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=FOC1_g10010148 {ECO:0000313|EMBL:ENH68975.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH68975.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB730233; ENH68975.1; -; Genomic_DNA.
DR STRING; 1229664.N4UG34; -.
DR VEuPathDB; FungiDB:FOC1_g10010148; -.
DR HOGENOM; CLU_001517_2_0_1; -.
DR OMA; YEEGHVH; -.
DR Proteomes; UP000016928; 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};
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:UP000016928};
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..580
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 755..999
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1090..1543
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
FT REGION 632..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1556 AA; 175480 MW; 219AE3BEAA98BAAC CRC64;
MSPPHTMTSN EVYLLPLNDD GSPQVQGEYI YLAPRSHEPV TVRFAIEGTS SICRHGSLWV
NIPAQGDEFR RDHFREFKLT PDFNRTLEIS IPIYQPGAYA FYTTYAELPD LKKELENSSE
QKENLNKTPL YYIDVAPRLK LDGRPLPLPA LSIFSVISKF MGKYPNDWER HLHGISDRGY
NMIHFTPLQV RGVSNSPYSL YDQLGWDPAC FPAGEEDVQK MVDSLERNHS LLSLTDIVLN
HTANNTKWLE EHPEAGYNLI TAPWLESAYQ LDTSLLELSD NLTKLGLPTV VKSTDDLLLI
MNAIKTEVLA KIRLWEYYAV DVDQDADEAV KAFSQGKKYT SEDASDFEKK LESAKSASIK
DQVEFFREFG LTGTDRMGER FRRRVKPDVA ASFLASSVGS SDEKAARAKI VEILEVLNVD
YYKEYDAEVD DILQQIFNRI KYVRLDDHGP KLGEINKENP LIEPYFTRLP KNETTSKLKP
EEMALVNNGW VWGGNALVDN AGPESRVYLR REVIVWGDCV KLRYGSGPED NPWLWEHMTK
YARTLAKYFA GLRIDNCHST PIHVAEHILD EARRVRPDLY VVAELFTGSE EMDYVFVKRL
GLSSLIREAM QAWSTGELSR LVHRHGGRPI GSFEVDEVSK SDVRTPSSSP TRLKNGETNG
HVSHSREIIR TIKPSPVHAL FMDCTHDNET PAQKRDARDT LPNAALVCMC SSATGSVMGY
DEIYPKLVDL VNETRLYTSA SSGTKPIKIG GGEEGIGGVK KLLNQIHTLM GKDGYDETHI
HHEDQYITVH RVHPESRKGY FLIAHTAFPG YGNGNGDFSP VHLTGTKARH LGSWMLEVDA
GEEATQQVLG DKKFLRGLPS RVKDVPGIRM EINGDDTTIT VRDKFPPGSI ALFETWIPAA
EHSSGLDNYV TSGSKAAWNE LSLTDLNFLM YRCEAEERAE SDGRDGAYDI PGHGKLVYAG
LQGWWSLLKN IIKDNNLAHP LCQNLRDGEW ALDYIIARLQ RISATPGNEA LAQPLRWLEE
RFDAIRKIPS FLLPRYFGLV LRTAYMASWD RSLELMNSSV RDGQWFLQSL AMVSVQQVGY
VKSASLWPFK LVPSLAAGLP HFAVEWARCW GRDVFIALRG LLIGTGRFDD AREHILAFAS
VLKHGMIPNL LSSGDAPRYN SRDSIWFFLQ CIQDYTRFAP EGLDILKAKV KRRFLPYDDT
WFPTNDERAY SKESTIEEVI QEALQRHASG MKYREANAGP QIDAQMKDEG FNQEIKVDWS
NGIIFGGNQF NCGTWMDKMG ESERAGSKGI PGTPRDGAAI EITGMLYSTL DWLAGLHEDG
KYAYAGVDKS EGGSISLADW AGLLKANFER CYYVPISPED DSKYDVNTPI VNRRGIYKDL
YKSGKEYEDY QLRPNFAIAM TTAPALFDPD HAMHALCVAD EALRGPQGMA TLDPADLNYR
PYYVNSEDSD DFATSKGRNY HQGPEWIWPT GFFLRALLKF DLKRRTTPEG RTEAFQQVTR
RLSGCKKMIQ ESPWAGLQEL TQKNGEYCAD SSPTQAWSAG CLIDLYMDAT EEQNKA
//
