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Database: UniProt
Entry: A0A1H3FN95_ALLWA
LinkDB: A0A1H3FN95_ALLWA
Original site: A0A1H3FN95_ALLWA 
ID   A0A1H3FN95_ALLWA        Unreviewed;       645 AA.
AC   A0A1H3FN95;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Glycogen synthase {ECO:0000256|ARBA:ARBA00019935, ECO:0000256|HAMAP-Rule:MF_00484};
DE            EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588, ECO:0000256|HAMAP-Rule:MF_00484};
DE   AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000256|ARBA:ARBA00031722, ECO:0000256|HAMAP-Rule:MF_00484};
GN   Name=glgA {ECO:0000256|HAMAP-Rule:MF_00484};
GN   ORFNames=SAMN05421644_1203 {ECO:0000313|EMBL:SDX92380.1};
OS   Allochromatium warmingii (Chromatium warmingii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=61595 {ECO:0000313|EMBL:SDX92380.1, ECO:0000313|Proteomes:UP000198672};
RN   [1] {ECO:0000313|Proteomes:UP000198672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 173 {ECO:0000313|Proteomes:UP000198672};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
CC       {ECO:0000256|ARBA:ARBA00002764, ECO:0000256|HAMAP-Rule:MF_00484}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + ADP + H(+); Xref=Rhea:RHEA:18189, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:57498, ChEBI:CHEBI:456216; EC=2.4.1.21;
CC         Evidence={ECO:0000256|ARBA:ARBA00001478, ECO:0000256|HAMAP-
CC         Rule:MF_00484};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|HAMAP-Rule:MF_00484}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010281, ECO:0000256|HAMAP-Rule:MF_00484}.
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DR   EMBL; FNOW01000020; SDX92380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3FN95; -.
DR   STRING; 61595.SAMN05421644_1203; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000198672; Unassembled WGS sequence.
DR   GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   HAMAP; MF_00484; Glycogen_synth; 1.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR011835; GS/SS.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   NCBIfam; TIGR02095; glgA; 1.
DR   PANTHER; PTHR46083; -; 1.
DR   PANTHER; PTHR46083:SF1; GLYCOGEN SYNTHASE 1; 1.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056, ECO:0000256|HAMAP-
KW   Rule:MF_00484};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00484}; Reference proteome {ECO:0000313|Proteomes:UP000198672};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          158..398
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          450..607
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   REGION          1..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..96
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         170
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   645 AA;  72015 MW;  764DE0643956711C CRC64;
     MAKKTPGTPK SKTSSTATST PVGSTPPPAP ATPVIKKTAA RKQTPDAALP AATISTPPPA
     AEIPAPPPVT AAPPPKPEPE PTIAPMPTPD DPAHTTKPAP RPLSEFGHAP TLALTAASTP
     AAQPEPEPPA APHEEPWHAP EPQWEPAAPP VWRPSLFIVH ITPELASVAK VGGLADVVFG
     LTRELAIRGN HVEIILPKYA SLRYDQIFEL HEVYQDLWVP WYNGAIHCTV FFGFVHGRKC
     FFIEPHSADN FFNRHSIYGF NDDVLRYAFF SRAAIEFLWK AGKHPDIIHC HDWQTSLVPV
     HLYEQYQALG MTHPRVCTTI HNFAHQGITG PDLLRATGLH RPEYFFSHTR LGDHRHPNAL
     NLLKGGIVYS NFVTTVSPRY AFETKDQGQG FGLEPVLHTH HIKYGGVVNG IDYDVWNPEV
     DPHIPVQYGV DSLERKYDNK RALRQRLMLA DNEKAIVAFI GRLDPQKGLE LVRHAIFNTL
     ERGAQFVLLG SSPDDRINAD FWGLKRMLND SPDCHLEIGF DEDLSHLIYA GADMMLVPSR
     FEPCGLTQLI ALRYGTIPVV RTVGGLADTI FDKDHSNRPL HERNGYVFND YDHRGLESAL
     GRAIDCYNAF PEHFRELMKN AMRCDYSWNQ PGQDYLNIYD YIRDV
//
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