FHYRK_ARATH
ID FHYRK_ARATH Reviewed; 379 AA.
AC Q84MD8; O65412;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Bifunctional riboflavin kinase/FMN phosphatase;
DE Includes:
DE RecName: Full=FMN phosphatase {ECO:0000303|PubMed:16183635};
DE EC=3.1.3.102 {ECO:0000269|PubMed:16183635, ECO:0000269|PubMed:22002057};
DE AltName: Full=FMN phosphohydrolase {ECO:0000303|PubMed:16183635};
DE Includes:
DE RecName: Full=Riboflavin kinase {ECO:0000303|PubMed:16183635};
DE EC=2.7.1.26 {ECO:0000269|PubMed:16183635, ECO:0000269|PubMed:22002057};
DE AltName: Full=Flavokinase {ECO:0000303|PubMed:16183635};
GN Name=FHY {ECO:0000303|PubMed:16183635};
GN Synonyms=FMN {ECO:0000303|PubMed:16183635};
GN OrderedLocusNames=At4g21470 {ECO:0000312|Araport:AT4G21470};
GN ORFNames=F18E5.90 {ECO:0000312|EMBL:CAA18711.1};
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, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16183635; DOI=10.1074/jbc.m500350200;
RA Sandoval F.J., Roje S.;
RT "An FMN hydrolase is fused to a riboflavin kinase homolog in plants.";
RL J. Biol. Chem. 280:38337-38345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RX PubMed=22002057; DOI=10.1074/jbc.m111.260885;
RA Rawat R., Sandoval F.J., Wei Z., Winkler R., Roje S.;
RT "An FMN hydrolase of the haloacid dehalogenase superfamily is active in
RT plant chloroplasts.";
RL J. Biol. Chem. 286:42091-42098(2011).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the hydrolysis of flavin-
CC mononucleotide (FMN) to riboflavin (vitamin B2) and the phosphorylation
CC of riboflavin to form (FMN) coenzyme. {ECO:0000269|PubMed:16183635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
CC Evidence={ECO:0000269|PubMed:16183635, ECO:0000269|PubMed:22002057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FMN + H2O = phosphate + riboflavin; Xref=Rhea:RHEA:35587,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58210; EC=3.1.3.102;
CC Evidence={ECO:0000269|PubMed:16183635, ECO:0000269|PubMed:22002057};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16183635};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.03 uM for riboflavin (at pH 7.5) {ECO:0000269|PubMed:16183635};
CC KM=2 uM for ATP (at pH 7.5) {ECO:0000269|PubMed:16183635};
CC KM=6.74 uM for FMN (at pH 7.5) {ECO:0000269|PubMed:16183635};
CC pH dependence:
CC Optimum pH is acidic (5.5-6.0) for FMN phosphatase activity and basic
CC for riboflavin kinase activity. {ECO:0000269|PubMed:16183635,
CC ECO:0000305|PubMed:22002057};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000305|PubMed:22002057};
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:16183635}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the HAD-like
CC hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavokinase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18711.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY878327; AAX98488.1; -; mRNA.
DR EMBL; AL022603; CAA18711.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161555; CAB81254.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84457.1; -; Genomic_DNA.
DR EMBL; BT006373; AAP21181.1; -; mRNA.
DR EMBL; AK227237; BAE99274.1; -; mRNA.
DR PIR; T05155; T05155.
DR RefSeq; NP_193878.2; NM_118267.5.
DR AlphaFoldDB; Q84MD8; -.
DR SMR; Q84MD8; -.
DR BioGRID; 13521; 1.
DR IntAct; Q84MD8; 1.
DR STRING; 3702.AT4G21470.1; -.
DR iPTMnet; Q84MD8; -.
DR PaxDb; Q84MD8; -.
DR PRIDE; Q84MD8; -.
DR ProteomicsDB; 228921; -.
DR EnsemblPlants; AT4G21470.1; AT4G21470.1; AT4G21470.
DR GeneID; 828232; -.
DR Gramene; AT4G21470.1; AT4G21470.1; AT4G21470.
DR KEGG; ath:AT4G21470; -.
DR Araport; AT4G21470; -.
DR TAIR; locus:2119647; AT4G21470.
DR eggNOG; KOG2914; Eukaryota.
DR eggNOG; KOG3110; Eukaryota.
DR HOGENOM; CLU_048437_3_1_1; -.
DR InParanoid; Q84MD8; -.
DR OMA; HEGWKEC; -.
DR OrthoDB; 1510544at2759; -.
DR PhylomeDB; Q84MD8; -.
DR BioCyc; ARA:AT4G21470-MON; -.
DR BioCyc; MetaCyc:AT4G21470-MON; -.
DR BRENDA; 3.1.3.102; 399.
DR SABIO-RK; Q84MD8; -.
DR UniPathway; UPA00276; UER00406.
DR PRO; PR:Q84MD8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84MD8; baseline and differential.
DR Genevisible; Q84MD8; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IDA:TAIR.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008531; F:riboflavin kinase activity; IDA:TAIR.
DR GO; GO:0009398; P:FMN biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR GO; GO:0006771; P:riboflavin metabolic process; IBA:GO_Central.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 2.40.30.30; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR InterPro; IPR023468; Riboflavin_kinase.
DR InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR PANTHER; PTHR22749; PTHR22749; 1.
DR Pfam; PF01687; Flavokinase; 1.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SMART; SM00904; Flavokinase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF82114; SSF82114; 1.
DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Flavoprotein; FMN; Hydrolase; Kinase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..379
FT /note="Bifunctional riboflavin kinase/FMN phosphatase"
FT /id="PRO_0000429025"
FT ACT_SITE 17
FT /note="Nucleophile; for FMN phosphatase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 19
FT /note="Proton donor; for FMN phosphatase activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 312
FT /note="Nucleophile; for riboflavin kinase activity"
FT /evidence="ECO:0000250"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 379 AA; 42110 MW; 01C279F602C86E3F CRC64;
MSMSNSLKKL SSCVLIDLDG TLINTDGVVG DILRKYLCKY GKQWDGRESL KIVGKTPVEA
ATTIVEDYEL PCKVDEFNSE FYPLFSAQMD KIKSLPGANR LIRHLKCHGV PVALASNSSR
ANIESKISYH EGWKECFSVI VGSDEVSKGK PSPDIFLEAA KRLKKDPADC LVIEDSVPGV
MAGKAAGTKV IAVPSLPKQT HLYTSADEVI NSLLDIRLEK WGLPPFQDWI ENTLPIDPWH
IGGPVIKGFG RGSKVLGIPT ANLSTKDYAD ELVEHPSGVY FGWAGLAKRG VFKMVMSIGW
NPYFNNKEKT IEPWLLHDFT EDFYGEELRL IIVGYIRPEA NFSSLESLIA KIHEDREVAE
KALDLPSYAK FKGDPYLTK
