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Database: UniProt
Entry: D8UBQ8_VOLCA
LinkDB: D8UBQ8_VOLCA
Original site: D8UBQ8_VOLCA 
ID   D8UBQ8_VOLCA            Unreviewed;       512 AA.
AC   D8UBQ8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000256|ARBA:ARBA00012460, ECO:0000256|RuleBase:RU362093};
DE            EC=2.7.7.27 {ECO:0000256|ARBA:ARBA00012460, ECO:0000256|RuleBase:RU362093};
DE   AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000256|RuleBase:RU362093};
GN   ORFNames=VOLCADRAFT_76956 {ECO:0000313|EMBL:EFJ42808.1};
OS   Volvox carteri f. nagariensis.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX   NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN   [1] {ECO:0000313|EMBL:EFJ42808.1, ECO:0000313|Proteomes:UP000001058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX   PubMed=20616280; DOI=10.1126/science.1188800;
RA   Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA   Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA   Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA   Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA   Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT   "Genomic analysis of organismal complexity in the multicellular green alga
RT   Volvox carteri.";
RL   Science 329:223-226(2010).
CC   -!- FUNCTION: This protein plays a role in synthesis of starch. It
CC       catalyzes the synthesis of the activated glycosyl donor, ADP-glucose
CC       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-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         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|ARBA:ARBA00010443,
CC       ECO:0000256|RuleBase:RU362093}.
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DR   EMBL; GL378378; EFJ42808.1; -; Genomic_DNA.
DR   RefSeq; XP_002956068.1; XM_002956022.1.
DR   AlphaFoldDB; D8UBQ8; -.
DR   STRING; 3068.D8UBQ8; -.
DR   GeneID; 9626567; -.
DR   KEGG; vcn:VOLCADRAFT_76956; -.
DR   eggNOG; KOG1322; Eukaryota.
DR   InParanoid; D8UBQ8; -.
DR   OrthoDB; 601725at2759; -.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000001058; Unassembled WGS sequence.
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   CDD; cd02508; ADP_Glucose_PP; 1.
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   NCBIfam; TIGR02091; glgC; 1.
DR   PANTHER; PTHR43523:SF12; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE LARGE SUBUNIT 1, CHLOROPLASTIC-RELATED; 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.
DR   PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR   PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362093};
KW   Chloroplast {ECO:0000256|RuleBase:RU362093};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362093};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU362093};
KW   Plastid {ECO:0000256|RuleBase:RU362093};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW   Starch biosynthesis {ECO:0000256|RuleBase:RU362093};
KW   Transferase {ECO:0000256|RuleBase:RU362093}.
FT   DOMAIN          82..357
FT                   /note="Nucleotidyl transferase"
FT                   /evidence="ECO:0000259|Pfam:PF00483"
SQ   SEQUENCE   512 AA;  55104 MW;  B32498FF1B321D71 CRC64;
     MKVHQTQARK LGSQALYFSH GPIVRKVVSA KAPAGSRRVQ VIRAQAVSAP VEAKVANGVS
     AAATAAPASY DYAGDISKTV LGIILGGGAG TRLYPLTKKR AKPAVPLGAN YRLIDIPVSN
     CLNSNVTKIY CLTQFNSASL NRHLSQAYNS SVGGYNTRGF VEVLAASQSS ANKSWFQGTA
     DAVRQYMWLF EEAVREGVED FLILSGDHLY RMDYRDFVRK HRESGAAITI AALPCAEKEA
     SAFGLMKIDD AGRVVEFAEK PKGEALQRMK VDTSILGVDP ATAQSKPFIA SMGIYVMSAK
     ALRELLLNRM PGANDFGNEV IPGAKDAGYK VQAYAFKGYW EDIGTVEAFY NANLALADPS
     KAQFSFYDKD APIYTMSRFL PPSKVLDADV SMSIIGDGCV IKAGSKIHNS IIGIRSLVGS
     DCIIDSAMMM GADYYETLEE CEYVPGCLPM GVGDGSVVRK AIIDKNARIG PKCQIINKDG
     VKEANREEQG FVIKDGIVVV IKDSCIPAGT II
//
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