ID A0A0C5WCR1_9FLAO Unreviewed; 470 AA.
AC A0A0C5WCR1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glycogen synthase {ECO:0000256|HAMAP-Rule:MF_00484};
DE EC=2.4.1.21 {ECO:0000256|HAMAP-Rule:MF_00484};
DE AltName: Full=Starch [bacterial glycogen] synthase {ECO:0000256|HAMAP-Rule:MF_00484};
GN Name=glgA {ECO:0000256|HAMAP-Rule:MF_00484};
GN ORFNames=AW14_04980 {ECO:0000313|EMBL:AJR03084.1};
OS Siansivirga zeaxanthinifaciens CC-SAMT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Siansivirga.
OX NCBI_TaxID=1454006 {ECO:0000313|EMBL:AJR03084.1, ECO:0000313|Proteomes:UP000032229};
RN [1] {ECO:0000313|EMBL:AJR03084.1, ECO:0000313|Proteomes:UP000032229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-SAMT-1 {ECO:0000313|EMBL:AJR03084.1,
RC ECO:0000313|Proteomes:UP000032229};
RA Young C.-C., Hameed A., Huang H.-C., Shahina M.;
RL Submitted (FEB-2014) 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|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; CP007202; AJR03084.1; -; Genomic_DNA.
DR RefSeq; WP_044637790.1; NZ_CP007202.1.
DR AlphaFoldDB; A0A0C5WCR1; -.
DR STRING; 1454006.AW14_04980; -.
DR KEGG; sze:AW14_04980; -.
DR PATRIC; fig|1454006.5.peg.975; -.
DR HOGENOM; CLU_009583_18_5_10; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000032229; Chromosome.
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; PTHR45825; GRANULE-BOUND STARCH SYNTHASE 1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR PANTHER; PTHR45825:SF11; STARCH SYNTHASE 1, CHLOROPLASTIC_AMYLOPLASTIC; 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:UP000032229};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 2..231
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 286..440
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT BINDING 15
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 470 AA; 53535 MW; 6255D66316D135A4 CRC64;
MNIIHISAEC YPVAKVGGLA DVVGALPKYQ NSLSNRSQVI MPFYDNKFTQ ENSFSSVYQG
ELFLGNTPYQ FKVLVLDQKP LDFDVFFIDV PELLFKDYVY SWDDTERFLA FQIAALDWLL
TWDIKPSIIH CHDHHTGLIP FMLQESYKYE VFRKTPNILT IHNAQYQGWF SHDKVGLIPP
FNFDHVGLLD WGGNINPLAA AIKCAWWITT VSPSYMEELK QAANGLEDLL KNEADKCSGI
LNGIDWKVWN PETDHYIVKN YSVATVDEGA QANKKYLCDT FNLDFNKPLF AFIGRLVDEK
GSDLFPEVFK IALEKNNLTI LLLGSGVPFV QSQLEALKKD FVGTYNAFIG YDEKLSHIIY
SGADFLLMPS RVEPCGLNQM YALRYGTIPI VRSIGGLKDT VTDIKEQDGF GICHDDVSVE
AINHAIFRAI DIYGDQKKYK QIRSKIMEID HSWDVSANQY INLYNSIKTN
//
