RIBF1_ARATH
ID RIBF1_ARATH Reviewed; 354 AA.
AC Q9FMW8; Q8LE72;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=FAD synthetase 1, chloroplastic {ECO:0000303|PubMed:18713732};
DE EC=2.7.7.2 {ECO:0000269|PubMed:18713732};
DE AltName: Full=AtRibF1 {ECO:0000303|PubMed:18713732};
DE AltName: Full=FAD pyrophosphorylase 1 {ECO:0000303|PubMed:18713732};
DE AltName: Full=FMN adenylyltransferase 1 {ECO:0000303|PubMed:18713732};
DE AltName: Full=Flavin adenine dinucleotide synthase 1 {ECO:0000303|PubMed:18713732};
DE Flags: Precursor;
GN Name=RIBF1 {ECO:0000303|PubMed:18713732};
GN OrderedLocusNames=At5g23330 {ECO:0000312|Araport:AT5G23330};
GN ORFNames=MKD15.19 {ECO:0000312|EMBL:BAB11188.1};
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBCELLULAR LOCATION.
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q969G6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=18.9 uM for FMN {ECO:0000269|PubMed:18713732};
CC KM=11.1 uM for ATP {ECO:0000269|PubMed:18713732};
CC Note=kcat is 1.08x10(-1) sec(-1) with FMN as substrate
CC (PubMed:18713732). kcat is 1.07x10(-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}.
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DR EMBL; EU687457; ACH56223.1; -; mRNA.
DR EMBL; AB007648; BAB11188.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93152.1; -; Genomic_DNA.
DR EMBL; AY085587; AAM62808.1; -; mRNA.
DR RefSeq; NP_568429.1; NM_122239.3.
DR AlphaFoldDB; Q9FMW8; -.
DR SMR; Q9FMW8; -.
DR STRING; 3702.AT5G23330.1; -.
DR PaxDb; Q9FMW8; -.
DR PRIDE; Q9FMW8; -.
DR ProteomicsDB; 236186; -.
DR EnsemblPlants; AT5G23330.1; AT5G23330.1; AT5G23330.
DR GeneID; 832397; -.
DR Gramene; AT5G23330.1; AT5G23330.1; AT5G23330.
DR KEGG; ath:AT5G23330; -.
DR Araport; AT5G23330; -.
DR TAIR; locus:2166973; AT5G23330.
DR eggNOG; ENOG502QVVU; Eukaryota.
DR HOGENOM; CLU_057424_1_0_1; -.
DR InParanoid; Q9FMW8; -.
DR OMA; CYEVANF; -.
DR OrthoDB; 882279at2759; -.
DR PhylomeDB; Q9FMW8; -.
DR BRENDA; 2.7.7.2; 399.
DR UniPathway; UPA00277; UER00407.
DR PRO; PR:Q9FMW8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMW8; baseline and differential.
DR Genevisible; Q9FMW8; 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 CDD; cd02064; FAD_synthetase_N; 1.
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 ATP-binding; Chloroplast; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..75
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 76..354
FT /note="FAD synthetase 1, chloroplastic"
FT /id="PRO_0000429026"
FT REGION 228..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 151
FT /note="N -> S (in Ref. 4; AAM62808)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="L -> I (in Ref. 4; AAM62808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39210 MW; 34F99F626EA07E45 CRC64;
MLCGGSRASV HLWDHRHPPR LGAKVLRKSS FMLRPCSAIS QQRIKSSFRS HCKTPRKIPA
PLDCFSQGDD HPELSAEGLS PVAGGIVALG KFDALHIGHR ELAIQAARIG TPYLLSFVGL
AEVLGWKPRA PIVAKCDRKR VLSSWASYCG NIAPVEFEIE FASVRHLNPQ QFVEKLSREL
RVCGVVAGEN YRFGYRASGD ASELVRLCKD FGISAYIINS VMDKNQVSVN TEEEDSKSKE
RGQVSSTRVR HALAAGDVRY VTELLGRPHR VISRTRTQDL TSKRGRISLQ TSSLLNLPPG
NGVYKACSLI VGDKHPISCK VIVDTSNLYI ETEEERFHNS DESQEFQLLG IEFG
