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Database: UniProt/TrEMBL
Entry: A1D064_NEOFI
LinkDB: A1D064_NEOFI
Original site: A1D064_NEOFI 
ID   A1D064_NEOFI            Unreviewed;       713 AA.
AC   A1D064;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=NFIA_039600 {ECO:0000313|EMBL:EAW24384.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW24384.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000256|RuleBase:RU363104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC         Evidence={ECO:0000256|RuleBase:RU363104};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|RuleBase:RU363104}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010686, ECO:0000256|RuleBase:RU363104}.
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DR   EMBL; DS027686; EAW24384.1; -; Genomic_DNA.
DR   RefSeq; XP_001266281.1; XM_001266280.1.
DR   AlphaFoldDB; A1D064; -.
DR   STRING; 331117.A1D064; -.
DR   EnsemblFungi; EAW24384; EAW24384; NFIA_039600.
DR   GeneID; 4592641; -.
DR   KEGG; nfi:NFIA_039600; -.
DR   VEuPathDB; FungiDB:NFIA_039600; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OMA; RDVRNHI; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03793; GT3_GSY2-like; 1.
DR   Gene3D; 6.10.260.10; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176:SF3; GLYCOGEN [STARCH] SYNTHASE; 1.
DR   PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW   ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          632..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          691..713
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  81113 MW;  319FF0995DFD9BBE CRC64;
     MDGEDTGPDP PKRDVRNHTL FEIATEVANR VGGIYSVLKS KAPVTTAEYG DRYTLIGPLN
     RASAAVEVEE LTPSNPRMVE TMNSMKERGI DMVYGRWLIE GAPRVLLIDT GTGYKYLDEW
     KGDLWNIAGI PSPASDTETN EAIVFGYLVA WFLGEFIAHE RRRAVVAHFH EWLAGVALPL
     TKKRHMDLTT IFTTHATLLG RYLCAGSVDF YNNLQHFDVD AEAGKRGIYH RYCIERAAAH
     SADVFTTVSH ITAFESEHLL KRKPDGVLPN GLNVKKFAAV HEFQNLHSQS KEKINDFVRG
     HFYGHNDFDL DNTLYVFTAG RYEFRNKGVD MFIEGLARLN HRLKASGSKT TVVAFIIMPA
     QTSSLTVEAL KGQAVVKSLR DTIEMIEKSI GKRMYERCLA WKEGDNMPDE KDLITSQDRV
     LLRRRLFAMK RHGLPPIVTH NMFNDHEDPI LNQIRRVELF NYPTDRVKVI FHPEFLNSSN
     PVLPLDYDDF VRGTHLGVFP SYYEPWGYTP AECTVMGVPS ITTNLSGFGC YMEELIENSS
     DYGIYIVDRR MKGVDDSVNQ LTEFMFNFTQ KSRRQRINQR NRTERLSDLL DWKRMGLEYV
     KARQLALRRA YPSSFDGAED YFDVIGGTEQ KLSRPLSVPG SPRDRSGVMT PGDFATIQEV
     KEGLDTEDYI AWRLPTSEEE EPDDHYFPLT LRTKKSSDRP SSPLDSIPVN GGR
//
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