ID Q4U168_MAIZE Unreviewed; 409 AA.
AC Q4U168;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 22-FEB-2023, entry version 69.
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:AAY42161.1};
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:AAY42161.1};
RN [1] {ECO:0000313|EMBL:AAY42161.1}
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; DQ019888; AAY42161.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4U168; -.
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:AAY42161.1"
SQ SEQUENCE 409 AA; 45561 MW; EBD7BC18402D1991 CRC64;
MQFALALDTN SGPHQIRSCE GDGIDRLEKL SIGGRKQEKA LRNRCFGGRV AATTQCILTS
DACPETLHSQ TQSSRKNYAD ANRVSAIILG GGTGSQLFPL TSTRATPAVP VGGCYRLIDI
PMSNCFNSGI NKIFVMSQFN STSLNRHIHR TYLEGGINFA DGSVQVLAAT QMPEEPAGWF
QGTADSIRKF IWVLEDYYSH KSIDNIVILS GDQLYRMNYM ELVQKHVEDD ADITISCAPV
DESRASKNGL VKIDHTGRVL QFFEKPKGAD LNSMRVETNF LSYAIDDAQK YPYLASMGIY
VFKKDALLDL LKSKYIQLHD FGSEILPRAV LDHSVQACIF TGYWEDVGTI KSFFDANLAL
TEQPSKFDFY DPKTPFFTAP RCLPPTQLDK CKMKDAFISD GCLLRECNI
//
