ID A5B1L9_VITVI Unreviewed; 681 AA.
AC A5B1L9;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00012664};
DE EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664};
GN ORFNames=VITISV_042207 {ECO:0000313|EMBL:CAN78555.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CAN78555.1};
RN [1] {ECO:0000313|EMBL:CAN78555.1}
RP NUCLEOTIDE SEQUENCE.
RA Velasco R., Zharkikh A., Troggio M., Cartwright D.A., Cestaro A., Pruss D.,
RA Pindo M., FitzGerald L.M., Vezzulli S., Reid J., Malacarne G., Iliev D.,
RA Coppola G., Wardell B., Micheletti D., Macalma T., Facci M., Mitchell J.T.,
RA Perazzolli M., Eldredge G., Gatto P., Oyzerski R., Moretto M., Gutin N.,
RA Stefanini M., Chen Y., Segala C., Davenport C., Dematte L., Mraz A.,
RA Battilana J., Stormo K., Costa F., Tao Q., Si-Ammour A., Harkins T.,
RA Lackey A., Perbost C., Taillon B., Stella A., Solovyev V., Fawcett J.A.,
RA Sterck L., Vandepoele K., Grando S.M., Toppo S., Moser C., Lanchbury J.,
RA Bogden R., Skolnick M., Sgaramella V., Bhatnagar S.K., Fontana P.,
RA Gutin A., Van de Peer Y., Salamini F., Viola R.;
RT "The first genome sequence of an elite grapevine cultivar (Pinot noir Vitis
RT vinifera L.): coping with a highly heterozygous genome.";
RL PLoS ONE 2:e1326-e1326(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
CC ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2
CC H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC Evidence={ECO:0000256|ARBA:ARBA00001697};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 1/2. {ECO:0000256|ARBA:ARBA00004917}.
CC -!- SUBUNIT: Heterotetramer. {ECO:0000256|ARBA:ARBA00011680}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000256|ARBA:ARBA00010443}.
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DR EMBL; AM443511; CAN78555.1; -; Genomic_DNA.
DR AlphaFoldDB; A5B1L9; -.
DR UniPathway; UPA00275; UER00404.
DR ExpressionAtlas; A5B1L9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-EC.
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:0042802; F:identical protein binding; IEA:EnsemblPlants.
DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02508; ADP_Glucose_PP; 1.
DR CDD; cd09209; Lumazine_synthase-I; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR00114; lumazine-synth; 1.
DR PANTHER; PTHR43523; GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR43523:SF17; INACTIVE GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE SMALL SUBUNIT 2, CHLOROPLASTIC; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 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:ARBA00022528};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 283..544
FT /note="Nucleotidyl transferase"
FT /evidence="ECO:0000259|Pfam:PF00483"
SQ SEQUENCE 681 AA; 74494 MW; 8ABE866D872B1755 CRC64;
MRIPILGFGQ AGIAIELKDR GSFVQTAAVR HLMGSLTRAE GLRFAVVSFS IPPQFLPFIF
ISSVYACDSM KLRYCFTMNL RNSAGEHTNK VVARFNEIVT KLLLEGALET FKRYSVKEED
IDVVWVPGSF EIGVVAERLG KSKKYQAILC IGAVIRGDTS HYDAVANSAA SGVLSAGLNS
GVPCIFGVLT CDDMDQALNR SGGKSGNKGA EAALTAIEMA SLFEHHLIHL LFLLTSSANL
RPKLPSLGGK QATVPPSLCV SNSQQSEHPA SLSRPANRQS VAAIVFGDGS ESQLYPLTKR
RSEGAVHIAG SYRLIDAVVS NCINSNITKI YALTQFNSTS LNSHLCRAYS GVGLEVVAAY
QSPEARGWFQ GTADAVRRCL WLVEEHPVAE FLVLPGYHLY RMDYQKLIQA HRQSKADITI
VALSAEISRE TGLGILEVNS ENQVVEFSKR SEKEPATIIS VKSPRKSNDN GYKKLASMGI
YVVKKEIMIK LLSEHFPKAN GFGSEVIPGA ISIGMKVEAF AFDGYWEDMR NIEAFYQANM
EITKKTDVGY KSRCEIRGTI VGLRTKIGDR AVIEDSVIMG SDIYQACFHL HLPLTSVCFH
QPEDELRRDM KGTGNDIPIG IGEDTHIRKA IVDKNARIGK QVLIMNRDNV QEGNREAHGY
TISEGIVVVL KGAVIPDGSI L
//
