RIBF2_ARATH
ID RIBF2_ARATH Reviewed; 367 AA.
AC Q8VZR0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=FAD synthetase 2, chloroplastic {ECO:0000303|PubMed:18713732};
DE EC=2.7.7.2 {ECO:0000269|PubMed:18713732};
DE AltName: Full=AtRibF2 {ECO:0000303|PubMed:18713732};
DE AltName: Full=FAD pyrophosphorylase 2 {ECO:0000303|PubMed:18713732};
DE AltName: Full=FMN adenylyltransferase 2 {ECO:0000303|PubMed:18713732};
DE AltName: Full=Flavin adenine dinucleotide synthase 2 {ECO:0000303|PubMed:18713732};
DE Flags: Precursor;
GN Name=RIBF2 {ECO:0000303|PubMed:18713732};
GN OrderedLocusNames=At5g08340 {ECO:0000312|Araport:AT5G08340};
GN ORFNames=F8L15 {ECO:0000312|EMBL:AL392174};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
RX PubMed=18713732; DOI=10.1074/jbc.m803416200;
RA Sandoval F.J., Zhang Y., Roje S.;
RT "Flavin nucleotide metabolism in plants: monofunctional enzymes synthesize
RT fad in plastids.";
RL J. Biol. Chem. 283:30890-30900(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
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 [4]
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).
CC -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN) to
CC form flavin adenine dinucleotide (FAD) coenzyme.
CC {ECO:0000269|PubMed:18713732}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC Evidence={ECO:0000269|PubMed:18713732};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17238;
CC Evidence={ECO:0000269|PubMed:18713732};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q969G6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.8 uM for FMN {ECO:0000269|PubMed:18713732};
CC KM=13.1 uM for ATP {ECO:0000269|PubMed:18713732};
CC Note=kcat is 1.28x10(-1) sec(-1) with FMN as substrate
CC (PubMed:18713732). kcat is 1.28x10(-1) sec(-1) with ATP as substrate
CC (PubMed:18713732). {ECO:0000269|PubMed:18713732};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000269|PubMed:18713732}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18713732}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8VZR0-1; Sequence=Displayed;
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DR EMBL; EU687458; ACH56224.1; -; mRNA.
DR EMBL; AL392174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED91286.1; -; Genomic_DNA.
DR EMBL; AY063929; AAL36285.1; -; mRNA.
DR EMBL; AY091253; AAM14192.1; -; mRNA.
DR RefSeq; NP_568192.2; NM_120918.5. [Q8VZR0-1]
DR AlphaFoldDB; Q8VZR0; -.
DR SMR; Q8VZR0; -.
DR STRING; 3702.AT5G08340.1; -.
DR PaxDb; Q8VZR0; -.
DR PRIDE; Q8VZR0; -.
DR ProteomicsDB; 236187; -. [Q8VZR0-1]
DR EnsemblPlants; AT5G08340.1; AT5G08340.1; AT5G08340. [Q8VZR0-1]
DR GeneID; 830732; -.
DR Gramene; AT5G08340.1; AT5G08340.1; AT5G08340. [Q8VZR0-1]
DR KEGG; ath:AT5G08340; -.
DR Araport; AT5G08340; -.
DR TAIR; locus:2150813; AT5G08340.
DR eggNOG; KOG2628; Eukaryota.
DR InParanoid; Q8VZR0; -.
DR OrthoDB; 882279at2759; -.
DR PhylomeDB; Q8VZR0; -.
DR BRENDA; 2.7.7.2; 399.
DR UniPathway; UPA00277; UER00407.
DR PRO; PR:Q8VZR0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8VZR0; baseline and differential.
DR Genevisible; Q8VZR0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006747; P:FAD biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR015864; FAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF06574; FAD_syn; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chloroplast; FAD; Flavoprotein; FMN;
KW Nucleotide-binding; Nucleotidyltransferase; Plastid; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..367
FT /note="FAD synthetase 2, chloroplastic"
FT /id="PRO_0000429027"
SQ SEQUENCE 367 AA; 40528 MW; 9278AC6D8152EA93 CRC64;
MLCGGSRVLQ HLSDHNHHNS IGLGLGFCGA KIVQLSSFFL RPSQAMAKSH HFSRKLRQRM
ISSFGSHCRT SGEVPILHNC FSQREDDPEL PVEGLSPVSG GIVALGKFDA LHIGHRELTI
QASRIGAPYL LSFVGMAEVL GWEPRAPIVA KCDRQRVLTS WASYCGDRAP EEYEIEFASV
RHLTPRQFVE KLSKELRVCG VVAGENYRFG YKASGDASEL VRLCEECGIT ACIINSVMDM
KQGSAKRDSG DSKDRGQVSS TRVRQALAAG DMRYVSELLG RAHRLILRVR TQDMPSERMI
SVPRSSILNL PPGIGIYKAC LLLVGDESSV PCTVVVDTSN IHVETEEVRL CNLDWSQEFR
LVSVEFG
