ID A0A0K9Q251_ZOSMR Unreviewed; 521 AA.
AC A0A0K9Q251;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=ZOSMA_115G00070 {ECO:0000313|EMBL:KMZ75371.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ75371.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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|ARBA:ARBA00000956,
CC ECO:0000256|RuleBase:RU362093};
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727, 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}.
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:KMZ75371.1}.
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DR EMBL; LFYR01000176; KMZ75371.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9Q251; -.
DR STRING; 29655.A0A0K9Q251; -.
DR OMA; RKWPLHT; -.
DR OrthoDB; 601725at2759; -.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
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:SF29; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 2, 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.
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 ECO:0000313|EMBL:KMZ75371.1};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000256|RuleBase:RU362093};
KW Reference proteome {ECO:0000313|Proteomes:UP000036987};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922,
KW ECO:0000256|RuleBase:RU362093};
KW Transferase {ECO:0000256|RuleBase:RU362093, ECO:0000313|EMBL:KMZ75371.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 90..367
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 521 AA; 58097 MW; 149FD2463A5936A8 CRC64;
MEITGVRMGI RPTGSAIMKL PGNIGYETSS VWGRKINLGC ALGRKWGRKC IRSSTQAVIT
SPVEETIGLN QTFQSPLFER LQANPKNVAA IILGGGEGTR LFPLTSTRAK PAVPVGGCYR
LVDIPMSNCI NSGINKIYVL TQFNSMSLNR HVSHTYNFGN GVNFGDGFVE VLAATQTPGE
KGKNWFQGTA DAVRQFIWLF EDMKNKNLDH VLILSGDQLY RMDYMDFLQK HIDTDADITV
SCVPMDESRA SDFGLMKIDN TGRIIKFSEK PKGANLEDMR VDTTVLGLSQ KESLESPYIA
SMGVYLFKTD VLLELLRSRY PTSNDFGSEI IPAAVNDQNV QAYLFNDYWE DIGTIKSFFD
ANLALTDQLP KFEFYDPMTP FYTSPRYLPP TKADKCRIKD SIISHGCFLR ECSIIHSVIG
DRSRLDYGVD MKDSMMMGAD HYQTEAEIAS MLAEGKVPIG IGQNTKLRNC IIDKNTRIGK
NVMITNQEDV QEADRPSEGF YIRMGITVIQ KNATIKDGTV I
//
