ID C8VTT8_EMENI Unreviewed; 1537 AA.
AC C8VTT8;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=ANIA_10060 {ECO:0000313|EMBL:CBF89663.1};
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321 {ECO:0000313|EMBL:CBF89663.1, ECO:0000313|Proteomes:UP000000560};
RN [1] {ECO:0000313|Proteomes:UP000000560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.J., Wortman J.R., Batzoglou S.,
RA Lee S.I., Basturkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M., Hynes M., Paoletti M., Fischer R., Miller B.,
RA Dyer P., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2] {ECO:0000313|Proteomes:UP000000560}
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139
RC {ECO:0000313|Proteomes:UP000000560};
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; BN001308; CBF89663.1; -; Genomic_DNA.
DR STRING; 227321.C8VTT8; -.
DR EnsemblFungi; CBF89663; CBF89663; ANIA_10060.
DR VEuPathDB; FungiDB:AN10060; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; C8VTT8; -.
DR OMA; YEEGHVH; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IBA:GO_Central.
DR GO; GO:0004135; F:amylo-alpha-1,6-glucosidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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:UP000000560};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 36..131
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 136..574
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 739..983
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1069..1527
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1537 AA; 173290 MW; 09412FAA880F1728 CRC64;
MSNETFYLLP LNDDGSPDVP GGFIYLPPPD HPKYSLRFLI EGSSSICRDG TLWINIPEIG
KSFDRQSFRP FKLYPDFSRN IQIDVPVTCP GSFAYYVTYS PLPEFTITSS APVKPARTPT
HYIDVSPRLS LAGEGIPLNA LSIFSVNSKF MGKYPEDWNQ YLNSISRRKY NMVHFTPLMK
RGASNSPYSI FDQLQFDDIA FPNGENDVQK LIKDMEEKHS LLSLADVVWN HTANNSKWLE
EHPEAGYSVE TAPWLEAALE LDTALLKFSH ELQKRGLPTD FKTVDDLTLV MNEVKNHVIE
DLCLWEFYVL DVKSNARRVI DEWKVSTNSD IERGRWAQLD LGAYKAWSLE DQASLIRQKG
VPTAGQILGR YSREIDTQLG VAIATALFGN FDATSSDLTA VENTLRKLLD VVNVPFYKEY
NSDVTEIMSQ LFNRIKYLRI DDHGPKLGPV TDQNPLIESY FTRLPLNEIT KKHSPKALAL
ANNGWIWNAD AMRDNAGPNS RAYLRREVIV WGDCVKLRYG DGPEDNPFLW DFMARYTRLM
AKYFSGFRID NCHSTPLVVA EYLIDEARKI RPDLAIFAEL FTGSEEADYI FVKRLGINAL
IREAMQAWSA GELSRLVHRH GGRPIGSFEL DLPSPGLDLS KSQVSGSERE IIRSIRPIPV
PALFMDCTHD NEMPAQKRTA TDTLPNAALV AMCDSAIGSV MGYDEVYPKI VDLVHETRLY
SFFDLPESPT LDELVNLKGI SGLKRLLNEL HTMMGQMGYD ETFIHHDGEY ITVHRVHPQT
RKGIFLIAHT AFPGQNSGAL LAPIHLAATR AKPIGSWLLK VQELSDDKER ALSDKVYLQG
LPSEVLKIEG ARIEETDRET IISVLDPFIP GSIALFETSI PSLEHADELS NDAITDGAVE
AFSELSLIDL NFVLYRCDAE ERDSSGGQDG VYDIPNHGPL VYAGLQGWWS ILEGIIRYNE
LGHPLCDHLR QGQWALDYIV NRLMKATKNP QYAALRRPAE WLEAKFQIVR GLPSFLLPRY
FAIIVQTAYV AAWNRGIQLL GDDVRVGQAF TQQLAMVSVQ QTGFVNSASL WPKKSVPSLA
AGLPHFATDW ARCWGRDVFI SLRGLLLCTG RFIDAKEHIL AFASVLKHGM IPNLLGSGKL
PRYNSRDSIW FLLQAIQDYT KMAPDGLELL QDKTPRRFLP YDDTWFPFDD PKAYSQTSTI
VDIIQEVFQR HAQGISFREY NAGPELDVQM KSEGFNIDIR VNWETGLIFG GSQHNCGTWQ
DKMGESEKAG NKGVPGTPRD GAAIEITGLL YSALKWVTEL NKQGLFPYDK VDIGNGKSIT
FEGWAAKVKT NFERCYYIPL DPNDDDQYDI DSGIVNRRGI YKDLYRSGKP YEDYQLRSNF
PIAMVVSPEL FDPSKALGAL AIADSVLAGP LGMATLDPSD LNYRPDYNNA EDSTDFATSK
GRNYHQGPEW VWLRGYFLRA LLYFDLARRK TADERTEAFQ QVTRRLAGCK KALRESPWKG
LTELTNRNGN HCADSSPTQS WSAGCLLDLY YDASRYI
//
