UGPA3_ARATH
ID UGPA3_ARATH Reviewed; 883 AA.
AC F4IY62; Q94B70; Q9LY42;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=UTP--glucose-1-phosphate uridylyltransferase 3, chloroplastic {ECO:0000305};
DE EC=2.7.7.9 {ECO:0000269|PubMed:19286968};
DE AltName: Full=UDP-glucose pyrophosphorylase 3 {ECO:0000303|PubMed:19286968};
DE Flags: Precursor;
GN Name=UGP3 {ECO:0000303|PubMed:19286968};
GN OrderedLocusNames=At3g56040 {ECO:0000312|Araport:AT3G56040};
GN ORFNames=F27K19_220 {ECO:0000312|EMBL:CAB87858.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION BY
RP PHOSPHATE STARVATION.
RX PubMed=19286968; DOI=10.1105/tpc.108.063925;
RA Okazaki Y., Shimojima M., Sawada Y., Toyooka K., Narisawa T., Mochida K.,
RA Tanaka H., Matsuda F., Hirai A., Hirai M.Y., Ohta H., Saito K.;
RT "A chloroplastic UDP-glucose pyrophosphorylase from Arabidopsis is the
RT committed enzyme for the first step of sulfolipid biosynthesis.";
RL Plant Cell 21:892-909(2009).
CC -!- FUNCTION: Involved in the biosynthesis of sulfolipids in the
CC chloroplast. Catalyzes the first committed step in sulfolipid
CC biosynthesis. Converts glucose 1-phosphate to UDP-glucose, the
CC precursor of the polar head of sulfolipid. In addition to glucose 1-
CC phosphate, can use galactose 1-phosphate, but with much lower activity.
CC No uridyltransferase activity with other hexose monophosphates.
CC Specific for UTP and cannot use ATP, CTP, and GTP.
CC {ECO:0000269|PubMed:19286968}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + H(+) + UTP = diphosphate + UDP-
CC alpha-D-glucose; Xref=Rhea:RHEA:19889, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:58885; EC=2.7.7.9;
CC Evidence={ECO:0000269|PubMed:19286968};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19286968};
CC -!- ACTIVITY REGULATION: Inhibited by pyrophosphate.
CC {ECO:0000269|PubMed:19286968}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for glucose 1-phosphate {ECO:0000269|PubMed:19286968};
CC KM=0.031 mM for UTP {ECO:0000269|PubMed:19286968};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:19286968}.
CC -!- INDUCTION: Induced by phosphate starvation.
CC {ECO:0000269|PubMed:19286968}.
CC -!- SIMILARITY: Belongs to the UDPGP type 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK68751.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL47372.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB87858.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163832; CAB87858.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79469.1; -; Genomic_DNA.
DR EMBL; AY042811; AAK68751.1; ALT_FRAME; mRNA.
DR EMBL; AY064665; AAL47372.1; ALT_FRAME; mRNA.
DR PIR; T49216; T49216.
DR RefSeq; NP_567031.1; NM_115462.4.
DR AlphaFoldDB; F4IY62; -.
DR SMR; F4IY62; -.
DR STRING; 3702.AT3G56040.1; -.
DR PaxDb; F4IY62; -.
DR PRIDE; F4IY62; -.
DR ProteomicsDB; 246391; -.
DR EnsemblPlants; AT3G56040.1; AT3G56040.1; AT3G56040.
DR GeneID; 824770; -.
DR Gramene; AT3G56040.1; AT3G56040.1; AT3G56040.
DR KEGG; ath:AT3G56040; -.
DR Araport; AT3G56040; -.
DR TAIR; locus:2082038; AT3G56040.
DR eggNOG; ENOG502QU00; Eukaryota.
DR HOGENOM; CLU_016716_0_0_1; -.
DR InParanoid; F4IY62; -.
DR OMA; CDRGIFQ; -.
DR OrthoDB; 769446at2759; -.
DR BRENDA; 2.7.7.9; 399.
DR SABIO-RK; F4IY62; -.
DR PRO; PR:F4IY62; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4IY62; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IBA:GO_Central.
DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046506; P:sulfolipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006011; P:UDP-glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039741; UDP-sugar_pyrophosphorylase.
DR InterPro; IPR002618; UDPGP_fam.
DR PANTHER; PTHR11952; PTHR11952; 1.
DR Pfam; PF01704; UDPGP; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Nucleotidyltransferase; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..883
FT /note="UTP--glucose-1-phosphate uridylyltransferase 3,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436030"
SQ SEQUENCE 883 AA; 99043 MW; F5F589A23E15EBF8 CRC64;
MANPQASPIL HHPQNHLSLF HFRTTTSPRS FSSLHFRKPL LFLSSSSSFS SKLQQSEQQC
NNHQVRHVST VPVEYSTPTP PESDDFLSEI DRLKSLLSKL DVSKDLRRKD AVIDADSRVR
RFFSENRGGL SKVFGYLGLN SNEMFLVKCV IAAGQEHALC MNYEEAFGEE EEEYTVRSSV
KNALYALVEM IERFDVNSSG YKGRREMGTV LDSEEIAHFR KFLTFLEEIE QFYDCIGGII
GYQVMVLELL HQSSKRRNTN RSQLVEESLG CQYLEMHTPS VLDLTQEEDY ASQAALWGIE
GLPDLGEIYP LGGAADRLGL IDSETGECLP AAMLAHCGRT LLEGLIRDLQ AREFLYFKLY
GKQCVTPVAI MTSAAKNNHE HVSSLCERLK WFGRGQSNFR LFEQPLVPAV SAEDGQWIVS
KPFVPVSKPG GHGVIWKLAY DKGVFNWFYD HGRKGATVRQ VSNVVAATDV TLLALAGIGL
RYNKKLGFAS CKRNAGATEG INVLMEKKNF DGKWEYGISC IEYTEFDKFD ISNRSPSSNG
LQADFPANTN ILYVDLHSAE LIGSSSNAKS LPNMVLNTKK RIEYLDQYGD YHSVMGGRLE
CTMQNIADNF FNKFPSRCHG SLEDKLDTYI VYNERRKVTS SAKKKKPHAS AALHQTPDGA
LLDILRNGYD LLTECDIKLP MIEANDKYVD SPPPYLILLH PALGPLWEVS RQKFKGGSIS
SCSELQLEIA EFSWNNVQVD GSLIVTAENA MGSTTPNDNG EPILQYGLRC GKCKLHNVNV
VNRGIDWNSK SNVYWRNDVN RLETCKIILH GNAEFEASNV TIEGHHVFEV PDGHKLKITS
GNAGLSINLE ALKEEVMETG SWYWNYQLNG SHIHLQQVEV SQS
