ID E1Z2N8_CHLVA Unreviewed; 420 AA.
AC E1Z2N8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460};
DE EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460};
GN ORFNames=CHLNCDRAFT_56519 {ECO:0000313|EMBL:EFN59695.1};
OS Chlorella variabilis (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=554065 {ECO:0000313|Proteomes:UP000008141};
RN [1] {ECO:0000313|EMBL:EFN59695.1, ECO:0000313|Proteomes:UP000008141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NC64A {ECO:0000313|EMBL:EFN59695.1,
RC ECO:0000313|Proteomes:UP000008141};
RX PubMed=20852019; DOI=10.1105/tpc.110.076406;
RA Blanc G., Duncan G., Agarkova I., Borodovsky M., Gurnon J., Kuo A.,
RA Lindquist E., Lucas S., Pangilinan J., Polle J., Salamov A., Terry A.,
RA Yamada T., Dunigan D.D., Grigoriev I.V., Claverie J.M., Van Etten J.L.;
RT "The Chlorella variabilis NC64A genome reveals adaptation to
RT photosymbiosis, coevolution with viruses, and cryptic sex.";
RL Plant Cell 22:2943-2955(2010).
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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; GL433835; EFN59695.1; -; Genomic_DNA.
DR RefSeq; XP_005851797.1; XM_005851735.1.
DR AlphaFoldDB; E1Z2N8; -.
DR STRING; 554065.E1Z2N8; -.
DR GeneID; 17359600; -.
DR KEGG; cvr:CHLNCDRAFT_56519; -.
DR eggNOG; KOG1322; Eukaryota.
DR InParanoid; E1Z2N8; -.
DR OMA; QYEECEA; -.
DR OrthoDB; 601725at2759; -.
DR Proteomes; UP000008141; Unassembled WGS sequence.
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:SF12; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR Pfam; PF00483; NTP_transferase; 2.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 95..219
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
FT DOMAIN 225..275
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 420 AA; 45239 MW; 31905480B1B59B87 CRC64;
MRCAELTAQP AGKGVGRHFR HCWEGQSLAS RSSALRGSQL AVPTPCRKTV RPKVAQPTQA
VAQVDAKTQA HAQKITVSTN GSEFGATEMS RTVLGIILGG GAGSRLYPLT KKRAKPAVPL
GANYRLIDIP VSNCINSGVN KIYCLTQFNS ASLNRHLSSA YNSNVGGYNS RGFVEVLAAS
QTTTTKEWFQ GTADAVRQYM WLFDEACRDG VEDFLILSGA AAAALPRRQQ HDFGSDIIPG
AKELGCKVQA HLFKGYWEDI GTVRAFYESN LALTDSPNPN FRCGGGRGGV GWVGGDVERS
ILGDGCIVEP DAKIHHSVIG LRSIIREGCV IEDSLLMGAD YYEQYEECEA FADCLPLGVG
KGTHIKGAIV DKNARIGKFC KIVNAEGIQE SFKTEEQGWV IRDGVVVVIK DSNIPDGTII
//
