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Database: UniProt
Entry: K9PQ42_9CYAN
LinkDB: K9PQ42_9CYAN
Original site: K9PQ42_9CYAN 
ID   K9PQ42_9CYAN            Unreviewed;       477 AA.
AC   K9PQ42;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=Cal7507_4296 {ECO:0000313|EMBL:AFY34672.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY34672.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY34672.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY34672.1,
RC   ECO:0000313|Proteomes:UP000010390};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-2012) 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; CP003943; AFY34672.1; -; Genomic_DNA.
DR   RefSeq; WP_015130474.1; NC_019682.1.
DR   AlphaFoldDB; K9PQ42; -.
DR   STRING; 99598.Cal7507_4296; -.
DR   KEGG; calo:Cal7507_4296; -.
DR   PATRIC; fig|99598.3.peg.4841; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_3; -.
DR   OrthoDB; 9808590at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000010390; 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:UP000010390};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00484}.
FT   DOMAIN          2..215
FT                   /note="Starch synthase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF08323"
FT   DOMAIN          268..406
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   477 AA;  54785 MW;  233CAB33C76235D9 CRC64;
     MRILFVAAEA APVAKVGGMG DVVGALPKIL RKMGHDVRIF LPYYGFLPDK MEIPKEPIWN
     GYAMFQDFAV YESVLPGTDV PLYLFGHPAF LPRRIYSGDD EDWRFTLFSN GAAEFCWNYW
     KPEIVHCHDW HTGMLPVWMN QDPDITSVFT IHNLAYQGPW RWYLEKITWC PWYMQGHNTM
     AAAVQYADKV NTVSPTYAEQ IKTPTYGETL EGLLSFISGK LSGIINGIDT EVYNPENDKY
     ITQNFTIDTL DKRKANKIAL QEEVGLEVNS NAFLVGMVTR LVEQKGLDLV IQILDRFLAY
     TDAQFVLLGT GDRYYETQMW QLASRYPGRM ATYLLYNDAL SRRIYAGTDA FLMPSRFEPC
     GISQMMSLRY GSVPIVRRTG GLVDTVSHFD PVNAAGTGYC FDRYEPLDLF TCMIRAWEGF
     RFKPQWQELQ KRGMSQDFSW YQSAKQYVKL YRSIYGLPEE EEPASPPELL LNEPVTK
//
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