ID F2SVW0_TRIRC Unreviewed; 1494 AA.
AC F2SVW0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 53.
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=TERG_06681 {ECO:0000313|EMBL:EGD90454.2};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD90454.2, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(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}.
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DR EMBL; GG700655; EGD90454.2; -; Genomic_DNA.
DR STRING; 559305.F2SVW0; -.
DR VEuPathDB; FungiDB:TERG_06681; -.
DR eggNOG; KOG3625; Eukaryota.
DR HOGENOM; CLU_001517_2_0_1; -.
DR InParanoid; F2SVW0; -.
DR OMA; HMREYTE; -.
DR OrthoDB; 1427975at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:UP000008864};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 42..107
FT /note="Eukaryotic glycogen debranching enzyme N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14699"
FT DOMAIN 110..542
FT /note="Glycogen debranching enzyme glucanotransferase"
FT /evidence="ECO:0000259|Pfam:PF14701"
FT DOMAIN 697..937
FT /note="Glycogen debranching enzyme central"
FT /evidence="ECO:0000259|Pfam:PF14702"
FT DOMAIN 1027..1481
FT /note="Glycogen debranching enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06202"
SQ SEQUENCE 1494 AA; 167860 MW; C861BB6A8AE93C51 CRC64;
MAPRTPITAT STCPADVSGV QSPAAVRGQQ SAVSIRELMG EYPSCELKPD FNKDIHVDIP
IAISGAFDYY FTYRQLPELF GPGSGSDTGK ETRSETYYLN VRPAITLRGK ALPLESLSIF
SVVSKFMGDY PKDWNKHLRG IGERGYNVVH FTPLVKRGAS NSPYSIYDQL EFEVCFPNGQ
KDVTEMTAKM EKDYGLLALT DVVWNHVAHN SQLLEDHPEV GYNIKNAPWL EAALELDTAL
LQYGKDLAKL GLPTEFKSED DISVVLDKAR ENVIDKIKLW EFYAIDVERD AAAALKSWES
DNFEDAELGN AEEIRGWSME KKAKFLRQKG VTNANRVLGR YDRKVDPKIA ASFLAAMFGR
HAESKVDAST VKVELRKLLD AVNLPLFKEF DKDVTTILDQ LFGRIKYLRV DDHGPKMGPV
SHESPLIETY FTRLSSSDKR DPRLLALANN GWVWNADAMK DNAGPDSRAY LLREVIVWGD
CVKLNYGTSR DDNPFLWDYM ADYSKLMAKY FVGFRIDNCH STPIPVAEYL LDEARRVRPN
LVVFAELFTG SEQTDYIFAK RLGLTGLIRE AMQAWSAGEL SRLVHRHGGR PIGSFEADLL
SHGDHRESNQ ILRQLQYTPL NALFMDCTHD NQMPAQKREA RDTLPNAALV AMCSSAIGSV
MGYDEIYPKH VDLVNETRLY SSAFSDGGVK SRTGEGGIGG IKRLLNELHT SMAVDCYDET
HIHHEGQYIT VHRVQPHTRK GVLLIAHTAF SGSKDEHGLD PIVLSGTNAK MIGAWKLEIV
SSNGDANTNK RFINGLYSKV SNIEGVSIEN DGNNTIIRVP AGLVPGSIAL LETWLPETNL
LKDLSTFITS DAEASFKSLD PVDLNFVLYK CNAEERDISD GSDGVYDIPN FGPLVYAGLQ
GWWSVLEGVI RNNDVGHPIC DNLRNGQWAL DFIVRRMHKA ASNEGYGRLK ELAEWLQGRF
DAIRKLPSFL LPRYFAIVVK TAYDAALARG IQLLGVTIEH GKDIIHELAM VSIQQVGFVN
SASLYPTKRV PCLAAGLPHF STDWARCWGR DVFISLRGLL LCTGRFEEAK EHILAFASVL
KHGLMPNLLS DGKAPRYNAR DAVWFFLQAI QDYTKIVPDG IQVLNEKVRR RFLPYDDTWF
SHDDSRAYRE TSTVAEIIQE IFQRHASGIT FREYNAGPNL DMQMKDEGFQ VDIRVDWETG
LVFGGNQWNC GTWMDKMGES TKSGNKGHPG TPRDGAAIEI SGLLYSTLSW LSTLADQGKF
PSKGVEVGSG KSISYAEWAA KIKSNFERCY YIPENPADDG KYDIDSRIVH RRGIYKDLYR
SGKPYEDYQF RPNFSVAMTV APDLFTLEKA LRTLELADSV LRGPMGMATL DPKDLNYNPY
YVNSEDSINF ATSKGRNYHQ GPEWLWPTGY FLRALMKFVL MRRDSPQDRT DVFQQLTNRL
EECKKALRTS PWRGLTELTN KSGELCADSS PTQAWSASCL IDLYYDASQL RKLE
//
