ID A0A261TT34_9BORD Unreviewed; 522 AA.
AC A0A261TT34;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=CAL25_08840 {ECO:0000313|EMBL:OZI52838.1};
OS Bordetella genomosp. 5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=1395608 {ECO:0000313|EMBL:OZI52838.1, ECO:0000313|Proteomes:UP000216913};
RN [1] {ECO:0000313|EMBL:OZI52838.1, ECO:0000313|Proteomes:UP000216913}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10456 {ECO:0000313|EMBL:OZI52838.1,
RC ECO:0000313|Proteomes:UP000216913};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZI52838.1}.
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DR EMBL; NEVP01000005; OZI52838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261TT34; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000216913; 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; 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:UP000216913};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 5..238
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 293..449
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 487..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 522 AA; 56286 MW; 8D388B0FA7206697 CRC64;
MATSRILIVA SEAYPLAKSG GLGDAVTGMA RALDAGGAHV TVLMPAYRGT RDQLSRVREV
AELRGLPGGP ARLIGGSCSQ GGFNVLLLEN DDLYDRSGLY ADEKGDYPDN ALRFAALAHA
AARIAQGQPG VPRPDVVHAH DWHAALVPAL MRARGCTTKS VLTIHNLAFQ GQFPTELANV
LAIPADMLGE QGIEAWGKLN FMKAGLRYAD VITTVSHTYS REILTPAFGC GLEGLLRQRV
ADLVPIANGI DDTLWNPAND RHLGVYRYSA RDARNKAHCK AALQQELGLP VKPDATLIAM
GSRLTGQKMA DVAARVLPRI LQAHDDVQVF ILGQGERHLE EAMRDMARAW PDRCAVRIGY
DEATAHHLHA GADILLHGSR FEPFGLTPLY AMRYGTLPIG SRVGGMADTI HDPGPRAPIA
AMRTANGLLF DGEGDEDMLS AIGRALHLRR QEPIWQAMQR NAMTADFGWD SAVQPYLQLF
DSLTSTTGAS AQPQRARRVS AWPYTVQRPA QPGTPPPAPA AL
//