ID A0A0L9V1Z2_PHAAN Unreviewed; 415 AA.
AC A0A0L9V1Z2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460};
DE EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460};
GN ORFNames=LR48_Vigan07g284900 {ECO:0000313|EMBL:KOM49145.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM49145.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727}.
CC -!- SUBUNIT: Heterotetramer. {ECO:0000256|ARBA:ARBA00011680}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR EMBL; CM003377; KOM49145.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9V1Z2; -.
DR STRING; 3914.A0A0L9V1Z2; -.
DR EnsemblPlants; KOM49145; KOM49145; LR48_Vigan07g284900.
DR Gramene; KOM49145; KOM49145; LR48_Vigan07g284900.
DR OMA; MEDSCAS; -.
DR Proteomes; UP000053144; Chromosome 7.
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:InterPro.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
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: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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 89..235
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 415 AA; 45793 MW; BFF583C4D725515A CRC64;
MMNATIATSD ASLIANKGFG IKRTSFWGES TKGNLNVRFP NTKPWKSFKA ACSKSGIARA
VYTDLDQEYP ALERSAFQSP KANPENVAAI ILGGGAGTRL FPLTRTRAKP AVPIGGSYRL
IDIPMSNCIN SGIRKVYVLT QFNSCSLNAH LSRTYNFGNG VNFGGGFVED AKNKNIENIM
IISGDHLCRM DYMQLVEKHS ENNADITVSC VPMDESGASD HGLMKIDRKG MITEFAYMFK
NYWKDIGTIK SFFEANLALT EQTPRFEFYD QKRPFFTSPR NNPPTRAIKC RIVDAIISHG
CYLNHCKVQH SIVGLRSRLE AGSELQDTMM MGADSYQTDS EIATLLETGK VPIGVGENTK
IRKCIIDKNA KIGRNVIIAN ADGVEEADRP EEGFYIRSGI VVVVKNATIK HGTVI
//
