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GLGA_PROMA
ID   GLGA_PROMA              Reviewed;         501 AA.
AC   Q7VBP0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Glycogen synthase {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 {ECO:0000255|HAMAP-Rule:MF_00484};
GN   Name=glgA {ECO:0000255|HAMAP-Rule:MF_00484}; OrderedLocusNames=Pro_1052;
OS   Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARG / CCMP1375 / SS120;
RX   PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA   Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA   Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA   Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA   Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT   "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT   nearly minimal oxyphototrophic genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAQ00097.1; -; Genomic_DNA.
DR   RefSeq; NP_875444.1; NC_005042.1.
DR   RefSeq; WP_011125204.1; NC_005042.1.
DR   AlphaFoldDB; Q7VBP0; -.
DR   SMR; Q7VBP0; -.
DR   STRING; 167539.Pro_1052; -.
DR   CAZy; GT5; Glycosyltransferase Family 5.
DR   EnsemblBacteria; AAQ00097; AAQ00097; Pro_1052.
DR   GeneID; 54200394; -.
DR   KEGG; pma:Pro_1052; -.
DR   PATRIC; fig|167539.5.peg.1102; -.
DR   eggNOG; COG0297; Bacteria.
DR   HOGENOM; CLU_009583_18_2_3; -.
DR   OMA; TWCPWYM; -.
DR   OrthoDB; 83240at2; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001420; 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   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   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   TIGRFAMs; TIGR02095; glgA; 1.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..501
FT                   /note="Glycogen synthase"
FT                   /id="PRO_0000188629"
FT   REGION          476..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..501
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         15
FT                   /ligand="ADP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:57498"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00484"
SQ   SEQUENCE   501 AA;  56943 MW;  DF1C02887C617B6F CRC64;
     MRVLFAAAEC APMVKVGGMG DVVASLPSAL AKLGHDVRLI IPGYSKLWGL LDISKDPIYT
     AQTMGAEFSV YETKHPTSNL PIYLVGHPVF DPERIYGGED EDWRFTFFAS ATAEFAWNVW
     KPQVLHCHDW HTGMIPVWMH QDPEISTVFT IHNLKYQGPW RWKLERMTWC PWYMSGDHTM
     AAAMLFADRV NAVSPTYSRE IRTSEYGESL EGLLNYISGK LRGILNGIDL DEWDPATDKA
     LPANFSSGKM STRKKNKEAL QRQMGLEVNN DKYLLGMVGR LVDQKGVDLL LQVSRRLLAY
     TDSQIVVLGT GDQILESALW ELAIDHPGRF AVFLTYDDYL SRLIYAGSDA FLMPSRFEPC
     GISQLLAMRY GSIPIVRNVG GLVDTVIPHD PINKSGTGFC FDRFEPIDFY TALVRSWEAF
     RHRRSWKELQ KRAMTQMYSW ERSAMEYETM YKEVSGYKEP SPDAIEVEKF SVGQDADPSL
     KNEKLSVGQD EDSSLKNERF I
 
 
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