ID C1FDK5_MICCC Unreviewed; 466 AA.
AC C1FDK5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460, ECO:0000256|RuleBase:RU362093};
DE EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460, ECO:0000256|RuleBase:RU362093};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU362093};
GN Name=ADG2A {ECO:0000313|EMBL:ACO68807.1};
GN ORFNames=MICPUN_78097 {ECO:0000313|EMBL:ACO68807.1};
OS Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO68807.1, ECO:0000313|Proteomes:UP000002009};
RN [1] {ECO:0000313|EMBL:ACO68807.1, ECO:0000313|Proteomes:UP000002009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
CC -!- FUNCTION: This protein plays a role in synthesis of starch. It
CC catalyzes the synthesis of the activated glycosyl donor, ADP-glucose
CC from Glc-1-P and ATP. {ECO:0000256|RuleBase:RU362093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:58601; EC=2.7.7.27;
CC Evidence={ECO:0000256|RuleBase:RU362093};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|RuleBase:RU362093}.
CC -!- SUBUNIT: Heterotetramer. {ECO:0000256|RuleBase:RU362093}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|RuleBase:RU362093}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443,
CC ECO:0000256|RuleBase:RU362093}.
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DR EMBL; CP001574; ACO68807.1; -; Genomic_DNA.
DR RefSeq; XP_002507549.1; XM_002507503.1.
DR AlphaFoldDB; C1FDK5; -.
DR STRING; 296587.C1FDK5; -.
DR GeneID; 8250079; -.
DR KEGG; mis:MICPUN_78097; -.
DR eggNOG; KOG1322; Eukaryota.
DR InParanoid; C1FDK5; -.
DR OMA; WGERISW; -.
DR OrthoDB; 601725at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000002009; Chromosome 1.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02508; ADP_Glucose_PP; 1.
DR CDD; cd04651; LbH_G1P_AT_C; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR02091; glgC; 1.
DR PANTHER; PTHR43523:SF12; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362093};
KW Chloroplast {ECO:0000256|RuleBase:RU362093};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362093};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU362093};
KW Plastid {ECO:0000256|RuleBase:RU362093};
KW Reference proteome {ECO:0000313|Proteomes:UP000002009};
KW Starch biosynthesis {ECO:0000256|RuleBase:RU362093};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362093}.
FT DOMAIN 33..312
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 466 AA; 50462 MW; E3F060C2BE4E79D9 CRC64;
MRLSKQVVAS AAAHQTDENS AQSAISNSKS VAAVILGGGA GTRLYPLTKS RAKPAVPIGG
AYRLIDVPMS NCLNSGISKM YILTQFNSVS LNRHLARTYN FGNGIMYGGN GFVEVLAATQ
TPGLGGKEWF QGTADAVRQY SWLFEDIKNK DVQDIVILSG DHLYRMDYMA FVARHREVNA
DITIGCLPMD DKRASDFGLM KIDDTGRITE FAEKPNGDAL KAMEVDTTIL GLTAEEATSS
PYIASMGIYV FKKSALLNFL NAEYPKDNDF GGEIIPKAAA DGYHVQAYLF NDYWEDIGTI
KSFFEANLAL AKNPPQFEFY DARAPIYTSP RFLPPAKVEK CHVKDAIISH GCSLADCSVE
DAIIGLRSQI GKGCTIKHAM IIGADYYETD EQKMALVEAG GVPVGIGEGC SISNAIIDKN
ARIGKNCIIT NAAGVEDLED EENGIYIRSG IVTILRNATI PDGTVI
//
