ID   GLGA2_NITOC             Reviewed;         491 AA.
AC   Q3JD12;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Glycogen synthase 2 {ECO:0000255|HAMAP-Rule:MF_00484};
DE            EC=2.4.1.21 {ECO:0000255|HAMAP-Rule:MF_00484};
DE   AltName: Full=Starch [bacterial glycogen] synthase 2 {ECO:0000255|HAMAP-Rule:MF_00484};
GN   Name=glgA2 {ECO:0000255|HAMAP-Rule:MF_00484};
GN   OrderedLocusNames=Noc_0771;
OS   Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS   11848 / C-107).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Nitrosococcus.
OX   NCBI_TaxID=323261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX   PubMed=16957257; DOI=10.1128/aem.00463-06;
RA   Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA   Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA   Vergez L.M., Ward B.B.;
RT   "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT   oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL   Appl. Environ. Microbiol. 72:6299-6315(2006).
CC   -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00484};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00484}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00484}.
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DR   EMBL; CP000127; ABA57284.1; -; Genomic_DNA.
DR   RefSeq; WP_002811391.1; NC_007484.1.
DR   AlphaFoldDB; Q3JD12; -.
DR   SMR; Q3JD12; -.
DR   STRING; 323261.Noc_0771; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   KEGG; noc:Noc_0771; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_4_6; -.
DR   InParanoid; Q3JD12; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000006838; 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; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..491
FT                   /note="Glycogen synthase 2"
FT                   /id="PRO_0000230249"
FT   BINDING         16
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   491 AA;  54828 MW;  1400C097AD5DAA6E CRC64;
     MYKILFATSE AHPLIKTGGL GDVAGILPIE LARLGLEAGI ILPAYPACKT HLKNLKEVAR
     LRLPAALEPV RILKGQLLEG PNPVWLVDSP AHFDRPGNPY LNEQGQDWPD NAARFTTFCR
     AVATLANSPE FDWQPDLIHC NDWQTGLIPP FLAPLRSRPA TLFTIHNLAY QGVFSRQQFD
     ALELPSAWWS PAALEFYNQI SFIKGGLVFA DWLTTVSPTY AKEILTPEFG CGLDGVLRGR
     SKRLTGILNG ADYQRWDPRH DPFIEKRYDQ TCWSHKASNK LALQRRYGLP EDDTLPVLGF
     VGRLVEQKGI DLILGALPKL LAEKIQVVFL GEGEERHQNA LQQLASRYPN QIGVSISYDE
     RLAHGVQAGA DIFLMPSRFE PCGLTQLYAL RYGTVPIARR TGGLSDTIVD ATEKNLRQEL
     ATGFTFTESS PSALLTAIQR ALACYAQSRQ WRRLALTGMA QNFSWQTSAK AYFDLYQQLV
     SQEFSCKNNV L
//