ID A0A1D6NI02_MAIZE Unreviewed; 395 AA.
AC A0A1D6NI02;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460};
DE EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460};
GN ORFNames=ZEAMMB73_Zm00001d044129 {ECO:0000313|EMBL:ONM39996.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM39996.1};
RN [1] {ECO:0000313|EMBL:ONM39996.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb159060_P003,
RC ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM39996.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:Zm00001eb159060_P003}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb159060_P003};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
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 -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR EMBL; CM007649; ONM39988.1; -; Genomic_DNA.
DR EMBL; CM007649; ONM39996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6NI02; -.
DR EnsemblPlants; Zm00001eb159060_T003; Zm00001eb159060_P003; Zm00001eb159060.
DR EnsemblPlants; Zm00001eb159060_T004; Zm00001eb159060_P004; Zm00001eb159060.
DR Gramene; Zm00001eb159060_T003; Zm00001eb159060_P003; Zm00001eb159060.
DR Gramene; Zm00001eb159060_T004; Zm00001eb159060_P004; Zm00001eb159060.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000007305; Chromosome 3.
DR ExpressionAtlas; A0A1D6NI02; baseline.
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; 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 PANTHER; PTHR43523:SF1; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 2, CYTOSOLIC; 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; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:ONM39996.1};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D6NI02};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922};
KW Transferase {ECO:0000313|EMBL:ONM39996.1}.
FT DOMAIN 1..241
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 395 AA; 44176 MW; 66364AA33610328D CRC64;
MSNCFNSGIN KIFVMSQFNS TSLNRHIHRT YLEGGINFAD GSVQVLAATQ MPEEPAGWFQ
GTADSIRKFI WVLEDYYSHK SIDNIVILSG DQLYRMNYME LVQKHVEDDA DITISCAPVD
ESRASKNGLV KIDHTGRVLQ FFEKPKGADL NSMRVETNFL SYAIDDAQKY PYLASMGIYV
FKKDALLDLL KSKYIQLHDF GSEILPRAVL DHSVQACIFT GYWEDVGTIK SFFDANLALT
EQPSKFDFYD PKTPFFTAPR CLPPTQLDKC KMKDAFISDG CLLRECNIEH SVIGVCSRVS
SGCELKDSVM MGADTYETEE EASKLLLAGK VPVGIGRNTK IRNCIIDMNA RIGKNVVITN
SKGIQEADHP EEGYYIRSGI VVILKNATIN DGSVI
//
