ID A0A2Z4FJH4_9DELT Unreviewed; 611 AA.
AC A0A2Z4FJH4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=DFR33_109114 {ECO:0000313|EMBL:TDP64453.1}, DN745_06935
GN {ECO:0000313|EMBL:AWV89083.1};
OS Bradymonas sediminis.
OC Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae; Bradymonas.
OX NCBI_TaxID=1548548 {ECO:0000313|EMBL:AWV89083.1, ECO:0000313|Proteomes:UP000249799};
RN [1] {ECO:0000313|EMBL:AWV89083.1, ECO:0000313|Proteomes:UP000249799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA350 {ECO:0000313|EMBL:AWV89083.1,
RC ECO:0000313|Proteomes:UP000249799};
RA Guo L.-Y., Li C.-M., Wang S., Du Z.-J.;
RT "Lujinxingia sediminis gen. nov. sp. nov., a new facultative anaerobic
RT member of the class Deltaproteobacteria, and proposal of Lujinxingaceae
RT fam. nov.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TDP64453.1, ECO:0000313|Proteomes:UP000294609}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28820 {ECO:0000313|EMBL:TDP64453.1,
RC ECO:0000313|Proteomes:UP000294609};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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; CP030032; AWV89083.1; -; Genomic_DNA.
DR EMBL; SNXT01000009; TDP64453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4FJH4; -.
DR KEGG; bsed:DN745_06935; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000249799; Chromosome.
DR Proteomes; UP000294609; 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:UP000249799};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 23..263
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 318..484
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 521..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 611 AA; 67986 MW; 922BA18EBF2F8CB6 CRC64;
MELAQLIRTK HSEKPSAAET LDILFASSEV APYSKTGGLA DVAASLPKAL NAMGHRVSII
TPLYKHLDPE ALHLSRRLQP LQVPRLGKLR KKVEATIWEG RTEGGVRIFF IQQDDFFGQN
DNLYGYGDGD LQSNPARFAF FSRAIVEFSM QYSVPVDVIH CNDWHTALAP IFREHYYAEE
MKDTACVLTI HNLAFQGRFD GEAMPETGLP KKYYAASEMR VDDAINYLKG GIKYASQVTT
VSPTYAEEIQ SDEGGFGLGE ALRDASAKLT GILNGADYSV WSPSVDHYID VQYDSDDLHG
KRKNKAALQA HFGLPDRPTL PLLAMVGRLT EQKGLDLLLP ALETLLDGFE HEKDSFQVVF
LGEGEQKYAD EITRLVEKFP RHIAAHLGYS EELAHKFQAA ADILLIPSRF EPCGLTQLYA
MRYGTLPLVH ATGGLKDTVI DPKRDKKTGD IIEGSTGFAF EKFDVDTLRE TIARATTRYR
NHRQWRPVIQ NAMERDFSWG NSASQYVDIY KKALGRPVEV KAAEKTEEKK ASPKKKSAAK
KTSKKSSSKK STKKADSKAT AKTDSAKKET TKKSAKKSEP KSSAKKDSTK KEGAKKKGAT
RRVPKKDDAK K
//
