ID   Q4U131_ZEAMH            Unreviewed;       409 AA.
AC   Q4U131;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   22-FEB-2023, entry version 66.
DE   RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460};
DE            EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460};
DE   Flags: Fragment;
GN   Name=Sh2 {ECO:0000313|EMBL:AAY42198.1};
OS   Zea mays subsp. huehuetenangensis (San Antonio Huista teosinte).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=112001 {ECO:0000313|EMBL:AAY42198.1};
RN   [1] {ECO:0000313|EMBL:AAY42198.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17305816; DOI=10.1111/j.1420-9101.2006.01264.x;
RA   Manicacci D., Falque M., Le Guillou S., Piegu B., Henry A.M.,
RA   Le Guilloux M., Damerval C., De Vienne D.;
RT   "Maize Sh2 gene is constrained by natural selection but escaped
RT   domestication.";
RL   J. Evol. Biol. 20:503-516(2007).
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; DQ019925; AAY42198.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4U131; -.
DR   SMR; Q4U131; -.
DR   UniPathway; UPA00152; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IEA:InterPro.
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   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   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   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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922}.
FT   DOMAIN          86..362
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
FT   NON_TER         409
FT                   /evidence="ECO:0000313|EMBL:AAY42198.1"
SQ   SEQUENCE   409 AA;  45521 MW;  9BD5CB41D38EA784 CRC64;
     MQFALALDTN SGPHQIRSCE GDGIDRLEQL SIGGRKQEKA LRNRCFGGRV AATTQCILTS
     DACPETLHSQ TQSSRKNYAD ANRVSAIILG GGTGSQLFPL TSTRATPAVP VGGCYRLIDI
     PMSNCFNSGI NKIFVMSQFN STSLNRHIHR TYLEGGINFA DGSVQVLAAT QMPEEPAGWF
     QGTADSIRKF IWVLEDYYSH KSIDNIVILS GDQLYRMNYM ELVQKHVEDD ADITISCAPV
     DESRASKNGL VKIDHSGRVL QFFEKPKGAD LNSMRVETNF LSYAIDDAQK YPYLASMGIY
     VFKKDALLDL LKSKYTQLHD FGSEILPRAV VDHSVQACIF TGYWEDVGTI KSFFDANLAL
     TEQPSKFDFY DPKTPFFTAP RCLPPTQLDK CKMKDAFISD GCLLRECNI
//