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
//