ID W1QEP6_OGAPD Unreviewed; 1512 AA.
AC W1QEP6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HPODL_05177 {ECO:0000313|EMBL:ESX00047.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESX00047.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESX00047.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:ESX00047.1}.
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DR EMBL; AEOI02000006; ESX00047.1; -; Genomic_DNA.
DR RefSeq; XP_013934853.1; XM_014079378.1.
DR STRING; 871575.W1QEP6; -.
DR GeneID; 25774600; -.
DR KEGG; opa:HPODL_05177; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR OMA; YEEGHVH; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000008673; Chromosome IV.
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 ECO:0000313|EMBL:ESX00047.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ESX00047.1}.
FT DOMAIN 39..130
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 134..554
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 714..954
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1029..1499
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1512 AA; 172313 MW; 54618D8CB303F4AF CRC64;
MTRIVLLRIN DTGEPVFENS RGVLTFPTCS KEESPLFTLR FYIVAGSQIT NKGTIWTDVP
KVESDPYRRD RYNKHPIASS LFQDITVDVP IYRPGSYCYY IGYHTLKEGD EEEFVTTRKF
YFVVPPSLFV QGQYLPLNAI SMQSVVSKWM GANHLDWDPV FAEISRKGYN MIHFTPLQTR
GESNSPYSIY DQLEFDRTAF ANGKTDVKNM VSRLEKEHGI LSMTDVVFNH TANNSTWIRE
NPDVGYNQET APHLIPAIEL DRLLLEFSKM MERHGYPTNI RNIEDLLKVM DGIKIHVLGE
LKLWEFYVVD VSEHLLELES QWDVSAGSCS FDISKDASLP DLARFVASKA CVKPFGLGPR
FGNRLDIQKF ASVLHYLYGD LSYPEVKGYA KKILDEINLP LYKQYDEDNG EILEQLYNRI
KYMRLEDHGP KLGEVTDENP LTEPYFTRFT DSSGKEWSLA NNGWIWGGNP LVDFASNESK
CYLRREVIVW GDCVKLRYGS RPEESPALWS RMIEYSRLSA SLFHGFRMDN CHSTPLHVAE
ALLDAAREVN PNLYVVAELF TGNEELDIIF VERLGISSLI REAMQAYSVG ELSRLVHRHG
GPPIGSFKWL PLDELAYPVH KEDYDTRLSE SFARKSEIPI PESVVSNAPH ALFMDCTHDN
ETPNEKRTVE DTLPNAALVS FCSCAVGTTF GYDECYPKLL DVVKEDKLYT YGSGIGAVKT
KLNKIRLELA NQSVEDLESN EMHVHHEDQF ITVHRTNAKT GKGYFLIART KFYQDSDQSL
APIVLSGTKV EHLFAYTLVR TGEDPVYKEG YMKSVPVRLQ EIGPIEVETR GQDSLIKLPS
NFPQGSIAVL STTIPGCDYQ LDRFVRSGAL EAAKNLTLLD INAILYRCES EERDASAGRE
GNYDVPGYGH LVYAGIQGWI SVLKHVIRNN DLAHPLADHL RSGTWALDYI PSRLTKYESY
GPAVSEFKVW LESRLYAVKK VPYFLVPRYF ALVVGIAYEA LRFQALKLMT PRIQRSTRFV
QSLAMVSVQM LAYMRSASIH PHSIIPSMAA GLPHFSYDYM RCWGRDIFIA LRGLLIVTGR
FEEAKDHILC FAKTLKHGLI PNLLGSGKEP RYNARDAAWW FLESIQNYIK WAPNGADILD
CKVKRRFPLD DTYIPVDDPL AFSYESTIRE IIYEIFSRHA RGIKFREANA GPQIDSQMKD
EGFNVEIHVD WETGLIHGGN QFNCGTWMDK MGESSLAGNK GYPGTPRDGA AVEINALLKS
ALRFAIELQK KGLFDYKELK TQTGDTVTFE HWNQLLQDNF ERCYFIPEDP AEDSKFVINP
DIVNRRGIYK DLFRSGKEYE DYQLRGNFPI AIAVAPELFT PSRALKAIQM ADRILRGPIG
LATLDPSDYN YRPYYLNSVD SMDFATAKGR NYHQGPEWCW ILGYFMRAFR HVHLSEHPAC
SENGSSTHYM HQLISKRLSG HKKWIDDSVW AGLTELTQKN GDFCADSSPT QAWSASCLLD
LYFDGWEEEN VR
//
