ID A0A1M6J9P5_MALRU Unreviewed; 1547 AA.
AC A0A1M6J9P5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN02745165_02357 {ECO:0000313|EMBL:SHJ43393.1};
OS Malonomonas rubra DSM 5091.
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Geopsychrobacteraceae; Malonomonas.
OX NCBI_TaxID=1122189 {ECO:0000313|EMBL:SHJ43393.1, ECO:0000313|Proteomes:UP000184171};
RN [1] {ECO:0000313|EMBL:SHJ43393.1, ECO:0000313|Proteomes:UP000184171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5091 {ECO:0000313|EMBL:SHJ43393.1,
RC ECO:0000313|Proteomes:UP000184171};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQZT01000008; SHJ43393.1; -; Genomic_DNA.
DR RefSeq; WP_072908935.1; NZ_FQZT01000008.1.
DR STRING; 1122189.SAMN02745165_02357; -.
DR OrthoDB; 9808590at2; -.
DR UniPathway; UPA00164; -.
DR Proteomes; UP000184171; 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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
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; PF00128; Alpha-amylase; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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:UP000184171};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00484}.
FT DOMAIN 301..716
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT BINDING 1075
FT /ligand="ADP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:57498"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00484"
SQ SEQUENCE 1547 AA; 178463 MW; F497FDAB63C409FC CRC64;
MPSLIREKLY PLGVHCGHSF WHHIRLTDQF RQVPPPPRTF FRQLIAEELR RSQSDSLSAA
ELELLATINQ VLLEIGRHFL RGRNCKVTRH QILVDKAVTP LPQFEKILLS FLQLFPNLPV
ELNQKTLTKL LQDCEEKQQL DELLLELFLL YTQSHNRAIR SADRLFLNEE RQLQQQSRYQ
QQLQQIDSAL PELDDGFARR PQSLLERLRE PLQQGGTLES QLQWLQQQWS EILPEELRFR
IDSAITIFQR EGITPDFPGE PQLDALNPAS QLDQEYANFT ADLDWMPRTV LLAKSTYVWL
QQLSRKYHWH IHRLDQIPDQ ELDELASFGF TSLWLIGIWH RSKASLKIKN LTGQQQVAAS
AYAIDDYRVA DDLGGDGALD NLRHRCQQRG IDLACDVVTN HTGIESAWLQ QHPDWFIQAQ
HPPYPGYQFS GIDLSENPDY SMQIEDGYYD HSEAAVVCRY QHRHTGEVRY IYHGNDGTHL
PWNDTVQLNY LLPQVREAMI ALIIRVAKQF RVIRFDAAMT LAKRHFQRLW FPLPGGGEGV
PSRSDYAMSK QEFDSLFPVE FWRELVDRVN QEVPDTLLVA EAFWLMEGYF VRTLGMHRVY
NSAFMNMLKR EENEKYRQTV KNILAFDPAI LQRFVNFMSN PDEEPAIEQF GRDDKYFCIA
TMLATMPGLP MFGHGQIEGY TEKYGMEYIS PRWQEEPDQH LIERHRRQIF PLLRQRALFS
GAEDFQLYDF ASEYGVEEHV YVYSNRLGDQ NTLVICNNSP HQIKGRIGNQ AHRADNRQTN
LTSACHIDLT ADFIIFTDIA LQQQYLLPTG HMTSGGEFEL QPYAARVLSH FTAVHDHDGR
WQQIWQRYGL SPRADLYTDY EAILLESVLE VNAKIFALEN VEHIQAEVVE LITQLLAELS
KPELQQRSSE DMLQLLIRVL FRSPQTLNEK LINEFVAFVD DQLNLQEKTH YNWLDRLFNQ
AEWRKLLKCN YYNEEDYCNQ EAFETLLTTF FLCSIHHSRE STSNNINGLD KTAFPLLINI
LKLRSKAEIS GYQVDNFLQS LDSGPEPSPV LPAATGGKYS MKILFVASEA TPFAKTGGLA
DVVGSLPRAL RQLGHDVRVV LPCYRSAERC GVTLRKGRKS VEIALDGKNY RGSLKQTSHD
GVPFWFIDCP QLFDRPELYG NVDGDYPDNS LRFGFFSRAV LEMIRRLDFR PDVIHLHDWQ
TSFIPALLRT EYRHNPFYGN IATLLTIHNL GYQGRFSPSI IQQLGLHESV GTPKGMEYFG
EMSVLKGGIN YSDVINTVSP TYCEEIKGQE QGHGFDGILR EREEDLHGII NGLDRRSWDP
ALDPALPTPF NAENLNGKRA CKRLVQKQLG LEIRHDVPIV ALISRLDRQK GINLVEQAWP
QLMEKDIQFV LLGSGDRNAM AFWREQQKQR PGKVSINLTF DEGLSRRIFA ASDLLLVPSL
YEPCGLTQMI ALHYGALPVV RRTGGLADTV IDATEHSRSG YGFVFDNFDS NEMLAAIDRA
LEIYPQRSRW LTLVKRGMTR DFSWNKSAIE YHELYTKARD YRQMPAA
//
