ID B7EVB8_ORYSJ Unreviewed; 479 AA. AC B7EVB8; DT 10-FEB-2009, integrated into UniProtKB/TrEMBL. DT 10-FEB-2009, sequence version 1. DT 08-MAY-2019, entry version 69. DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|RuleBase:RU362093}; DE EC=2.7.7.27 {ECO:0000256|RuleBase:RU362093}; DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU362093}; OS Oryza sativa subsp. japonica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39947 {ECO:0000313|EMBL:BAG96315.1}; RN [1] {ECO:0000313|EMBL:BAG96315.1} RP NUCLEOTIDE SEQUENCE. RA Kikuchi S., Satoh K., Nagata T., Kawagashira N., Doi K., Kishimoto N., RA Yazaki J., Ishikawa M., Yamada H., Ooka H., Hotta I., Kojima K., RA Namiki T., Ohneda E., Yahagi W., Suzuki K., Li C., Ohtsuki K., RA Shishiki T., Otomo Y., Murakami K., Iida Y., Sugano S., Fujimura T., RA Suzuki Y., Tsunoda Y., Kurosaki T., Kodama T., Masuda H., RA Kobayashi M., Xie Q., Lu M., Narikawa R., Sugiyama A., Mizuno K., RA Yokomizo S., Niikura J., Ikeda R., Ishibiki J., Kawamata M., RA Yoshimura A., Miura J., Kusumegi T., Oka M., Ryu R., Ueda M., RA Matsubara K., Kawai J., Carninci P., Adachi J., Aizawa K., Arakawa T., RA Fukuda S., Hara A., Hashidume W., Hayatsu N., Imotani K., Ishii Y., RA Itoh M., Kagawa I., Kondo S., Konno H., Miyazaki A., Osato N., Ota Y., RA Saito R., Sasaki D., Sato K., Shibata K., Shinagawa A., Shiraki T., RA Yoshino M., Hayashizaki Y.; RT "Collection, Mapping, and Annotation of Over 28,000 cDNA Clones from RT japonica Rice."; RL Science 301:376-379(2003). CC -!- FUNCTION: This protein plays a role in synthesis of starch. It CC catalyzes the synthesis of the activated glycosyl donor, ADP- CC glucose 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- CC glucose + 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|RuleBase:RU362093}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK103906; BAG96315.1; -; mRNA. DR RefSeq; XP_015650971.1; XM_015795485.1. DR SMR; B7EVB8; -. DR EnsemblPlants; Os08t0345800-01; Os08t0345800-01; Os08g0345800. DR GeneID; 4345339; -. DR Gramene; Os08t0345800-01; Os08t0345800-01; Os08g0345800. DR eggNOG; ENOG410IMYM; Eukaryota. DR eggNOG; COG0448; LUCA. DR HOGENOM; HOG000278604; -. DR OrthoDB; 806744at2759; -. DR UniPathway; UPA00152; -. DR ExpressionAtlas; B7EVB8; baseline and differential. 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 Gene3D; 3.90.550.10; -; 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 Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR02091; glgC; 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|RuleBase:RU362093}; KW Chloroplast {ECO:0000256|RuleBase:RU362093}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362093}; KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU362093}; KW Plastid {ECO:0000256|RuleBase:RU362093}; KW Starch biosynthesis {ECO:0000256|RuleBase:RU362093}; KW Transferase {ECO:0000256|RuleBase:RU362093}. FT DOMAIN 51 324 NTP_transferase. {ECO:0000259|Pfam: FT PF00483}. SQ SEQUENCE 479 AA; 52950 MW; 3CD9D4D6746AC84E CRC64; MNVLASKIFP SRSNVASEQQ QSKREKATID DAKNSSKNKN LDRSVDESVL GIILGGGAGT RLYPLTKKRA KPAVPLGANY RLIDIPVSNC LNSNISKIYV LTQFNSASLN RHLSRAYGNN IGGYKNEGFV EVLAAQQSPD NPNWFQGTAD AVRQYLWLFE EHNVMEFLIL AGDHLYRMDY EKFIQAHRET DSDITVAALP MDEKRATAFG LMKIDEEGRI VEFAEKPKGE QLKAMMVDTT ILGLDDVRAK EMPYIASMGI YVISKNVMLQ LLREQFPGAN DFGSEVIPGA TNIGMRVQAY LYDGYWEDIG TIEAFYNANL GITKKPVPDF SFYDRSAPIY TQPRHLPPSK VLDADVTDSV IGEGCVIKNC KIHHSVVGLR SCISEGAIIE DSLLMGADYY ETEADKKLLG EKGGIPIGIG KNCHIRRAII DKNARIGDNV KIINVDNVQE AARETDGYFI KSGIVTVIKD ALLPSGTVI //