ID A0A095VKM5_9BURK Unreviewed; 521 AA.
AC A0A095VKM5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=JL37_28720 {ECO:0000313|EMBL:KGD86893.1};
OS Achromobacter sp. RTa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1532557 {ECO:0000313|EMBL:KGD86893.1, ECO:0000313|Proteomes:UP000035841};
RN [1] {ECO:0000313|EMBL:KGD86893.1, ECO:0000313|Proteomes:UP000035841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RTa {ECO:0000313|EMBL:KGD86893.1,
RC ECO:0000313|Proteomes:UP000035841};
RA Prabhakaran M., Cougar B., Weirick T., Fathepure B.Z.;
RT "Genome sequences of the lignin degrading proteobacteria.";
RL Submitted (AUG-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|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:KGD86893.1}.
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DR EMBL; JPYO01000046; KGD86893.1; -; Genomic_DNA.
DR RefSeq; WP_043548588.1; NZ_JPYO01000046.1.
DR AlphaFoldDB; A0A095VKM5; -.
DR eggNOG; COG0297; Bacteria.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000035841; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 7..239
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 300..455
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
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 521 AA; 55774 MW; 703D3925D6A09C28 CRC64;
MATTRTLIVA GEAFPLAKTG GLGDAITGMA RALAQADMPV AILLPAYRGV RARLQEIRVV
APLHNLPTGD ARLLAGRCPQ SGLDFLLLEN DALYDRAGIY LDEAGREYAD SALRYAALAH
AAVRVAGGLP GIVTPNIVHA HDWHAGLVPL LMRAYGLHDT RSVMTIHNLA FQGRFPMECA
ASLGIPEPYR GSDGAEAWGQ LNFLKAGIRY ADRVTTVSHT YAREIMTPAF GCGLDELLRR
RAGDLLPIPN GIDNILWNPA RDPHLGALRF SVSDLSNKAR CKAALQHEFG LAVDAGATLM
SMGSRLTEQK MADVAVQALP EALERHPNLQ IAILGQGDHQ LEDALRALAQ RYPGRCAAHI
GYDEPAAHRL HAGSDILLHA SRFEPFGLTP LYAMRYGALP IGSRVGGMAD TIEDPGPRAP
LSAMASANGL LFDGDSPAAM GEAIARAVHL REHAMLWRIM QRNAMSADFG WRSAIGLYAS
LYRSLAGADF RSAAPARADR ALGAAALRAR RRSGSAMPAP V
//
