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Database: UniProt
Entry: W2U1V8_NECAM
LinkDB: W2U1V8_NECAM
Original site: W2U1V8_NECAM 
ID   W2U1V8_NECAM            Unreviewed;       356 AA.
AC   W2U1V8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=NECAME_00166 {ECO:0000313|EMBL:ETN87307.1};
OS   Necator americanus (Human hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC   Necator.
OX   NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN87307.1, ECO:0000313|Proteomes:UP000053676};
RN   [1] {ECO:0000313|Proteomes:UP000053676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24441737; DOI=10.1038/ng.2875;
RA   Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA   Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA   Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA   Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA   Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT   "Genome of the human hookworm Necator americanus.";
RL   Nat. Genet. 46:261-269(2014).
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}.
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DR   EMBL; KI657455; ETN87307.1; -; Genomic_DNA.
DR   RefSeq; XP_013309534.1; XM_013454080.1.
DR   AlphaFoldDB; W2U1V8; -.
DR   SMR; W2U1V8; -.
DR   STRING; 51031.W2U1V8; -.
DR   EnsemblMetazoa; NECAME_00166; NECAME_00166; NECAME_00166.
DR   GeneID; 25340210; -.
DR   KEGG; nai:NECAME_00166; -.
DR   CTD; 25340210; -.
DR   OMA; VNMAHIF; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000053676; 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; 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; 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:UP000053676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
SQ   SEQUENCE   356 AA;  40292 MW;  48C2C4E2340DCBDB CRC64;
     MSGSTSPARI SRRLSSTKIA KQLAGLSLRS DDIMDQGDTA RHEGRFVFEC SWEVANKVGG
     IYTVLRTKAP ISTEELGDQY CMLGPYNEDR VEVLEPDNAA MKYALEHARD CGFKMWSVTK
     VGIPWHDREA NDCVILGFMV AIFLQKFAEA IASSEPLIVA HFHEWQSAAG LIMSRLWKLN
     ISLVFTTHAT LIGRHLCAGG VDLYNNLSKI DVDREAGERQ IYHRYCIERA AVHLAHVFTT
     VSEVTGLEAE HLLGRKPDIL TPNGLNVVKF SAIHEFQNLH AIAKEKIHDF IRGHFYGNLN
     FDLDKTLYFF TAGRYEFTNK GGDFFIEALA RLNYKLQTLR IILLERYSIA QLLKVH
//
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