ID A0A0N1HN60_9EURO Unreviewed; 576 AA.
AC A0A0N1HN60;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN ORFNames=AB675_2973 {ECO:0000313|EMBL:KPI36387.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI36387.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI36387.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI36387.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00043769};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC Evidence={ECO:0000256|ARBA:ARBA00043769};
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}.
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:KPI36387.1}.
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DR EMBL; LFJN01000031; KPI36387.1; -; Genomic_DNA.
DR RefSeq; XP_017996350.1; XM_018142986.1.
DR AlphaFoldDB; A0A0N1HN60; -.
DR STRING; 1664694.A0A0N1HN60; -.
DR GeneID; 28734866; -.
DR OrthoDB; 9432at2759; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000038010; 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 Gene3D; 6.10.260.10; -; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR008631; Glycogen_synth.
DR PANTHER; PTHR10176:SF3; GLYCOGEN [STARCH] SYNTHASE; 1.
DR PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR Pfam; PF05693; Glycogen_syn; 2.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW ECO:0000256|RuleBase:RU363104};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT REGION 530..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 576 AA; 65199 MW; 2C4298010E8CE62F CRC64;
MNGDSGKRDV KNHLLFEIAT EVANRVGGIY SVLKSKAPVS TAEYGDRYVL IGPLNKASAA
VEVEQIEPPQ GHLRDTIAAM QERGIEIMYG RWLIEGAPRV LLINTGTGYR WLDEWKGDLW
TQAGIPSPAS DHETNEAIVF GYLVAWFLGE FVSREQTRAV IAHFHEWLAA VAIPLTKKRQ
MDLTTIFTTH ATLLGRYLCA GSVDFYNNLQ YFDVDSEAGK RGIYHRYCIE RAGAHSCDVF
TTVSHITAFE SEHLLKRKPD GVLPNGLNVK KFSAVHEFQN LHSVQKEKIH EFVRGHFYGH
LDFDLENTLY FFTAGRYEYR NKGVDMFIES LARLNHRLKT SGTKTTVIAF MIMPAQTSSL
SVESLKGQAV TKSLADTVGN IERGIGRRLF ERAVHWKEGD PMPDEKELIT PADRVVLRRR
LFAMKRSGLP PIVTHNMELI ENSSDYGIYI VDRRTKGVDD SVNQLTDFMF DFAQKSRRQR
INQRNRTERL SDLLDWKRMG MEYVKARQLA LRRAYPASFQ EEAEFDDIIG GTEQKISRPL
SEEEEPDEYA FPLTLKKPKT GADSPAPLVG GANGAS
//
