ID K2RJH2_MACPH Unreviewed; 1545 AA.
AC K2RJH2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=MPH_08078 {ECO:0000313|EMBL:EKG14803.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG14803.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG14803.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG14803.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKG14803.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHHD01000337; EKG14803.1; -; Genomic_DNA.
DR STRING; 1126212.K2RJH2; -.
DR VEuPathDB; FungiDB:MPH_08078; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; K2RJH2; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000007129; 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:UP000007129};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..131
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 135..579
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 741..985
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1075..1528
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1545 AA; 174672 MW; B58584F0C95DDE43 CRC64;
MSSTVYLLPL TDSGCPDVPG NYIYLPPPTN PAYIIRFAIE GTSSICREGS LWVNIPAEGE
QFQRDRFREF KLRPDFNGTI TFDCPVHYAG AFAFYSTYTP LPEFSPYPVS TPKPTKTPTY
YIDVCPRLMM NDQLIQLDSL SIFSVISKFM GKYPDDWDKH LRGISQRGYN MIHFTPLMMR
GNSNSPYSIY DQHRFDKHFF PNGEKDIAEL VTKMEKEFNL FALTDVVWNH TANNSKWLEE
HPEAGYNCET APHLQAALEL DDALLQLGQD LASKGLPTTI HSIDDLNKIM EAVKSDVIAG
LKLWQFYVVD VERDTKAIVK AWTEGEITFP EGGFGKLGVG GLDEVKDWTL KQKAGWLIQH
ALSDGDTLGD RFQRKIDART GAALLAALFG RYDSRNHSTP DERAAQGTIQ KFLDEVNLEF
YKEYDADVAT IIEQLHNRIK YVRLDDHGPK LGPITNRNPL IETYFTRLPK NETTKKHNPR
ALALVNNGWI WAADAMKDNA GPQSRAYLRR EVIVWGDCVK LRYGSGPQDN PFLWDFIAKY
TRLMAKYFVG FRIDNCHSTP IHVAEHMLDE ARKVRPDLVV GAELFTGSED MDFVFCRRLG
ISFLIREAMQ AWSTQELSRL VHRHAGIPIG SFELDEVSNA DPSAQTNGTA KREIIRRIRQ
SPVHALFMDC THDNEVPAQK RDARDTLPNA ALVAMCACAT GSVMGYDEIY PQLIELVHET
RLYSSPYSTS GEVKVQAAEG GIGNIKKLLN QIHTLMGQEG YDETFIHHDR EFITVHRVHP
KTRKGYFLIA HTAFPGYGDG NGGFPPVNLP GTQAKQIGSW FLEVEANPDV KARVIGDKKT
LRGLPSRTKD LEGVKIESSD EKTTITIPDF FPPGSIALFE TSVPSCEHAD GLDEFVTSGA
SEAFKECSLL DLNHVLYRCD PEERDYSGGN DGTYTIPGHG TLVYAGLQGW WSVLRDVIRY
NQLGHPICDH LRQGQWALDY CVGRLERLSK LPGYKNLQGP ASWLQERFDA IRKIPSFMLP
RYFALTIQTA YNAAVDRSIG LLNDNVRNGQ KFLQSLSLVS IQVTGHMNNA SLWPTKSVPS
MAAGLPHFAS DWARCWGRDI FISLRGLYLG TGRYADAREH IMAFASVVKH GMIPNLLSSG
KLPRYNSRDS VWFYLQNIQD YTKIVPDGLN ILQESVKRRF LPYDDTWFPH DDPKAYSKSS
TIEDVIQECL QRHASGMSFR EYNAGPALDS QMKPEGFNIE IHPDWKTGII FGGNQWNCGT
WMDKMGESEK AGNKGYPGTP RDGAAIEITG MLYSCLKWVD GLNKEGKYKY DGVDIEGGRI
TFAEWAAKIK DNFEWAYYVP REPSEDKDYD VNSSIVNRRG IYKDLYKSGK EYEDYQLRPN
FPIAMTVAPD LFDPEKALYA LHVADKALRG PTGMATLDPS DLNYRPNYIN SEDSTDFHTA
KGRNYHQGPE WLWPTGFFLR AFLKFDLLRR KTPEERVETF QQITRRLRGC MDAIKESPWA
GLTELTNKDG SFCGDSSPTQ AWSASCLIDL YQDAKEFGEE FAASQ
//
