FHY1C_ARATH
ID FHY1C_ARATH Reviewed; 245 AA.
AC Q84VZ1; Q8LCB6; Q9MA00;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Flavin mononucleotide hydrolase 1, chloroplatic {ECO:0000303|PubMed:22002057};
DE Short=AtcpFHy1 {ECO:0000303|PubMed:22002057};
DE EC=3.1.3.102 {ECO:0000269|PubMed:22002057};
DE AltName: Full=5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase {ECO:0000305|PubMed:27490826};
DE Short=AtcpFHy1/PyrP1 {ECO:0000303|PubMed:27490826};
DE EC=3.1.3.104 {ECO:0000269|PubMed:24123841, ECO:0000269|PubMed:27490826};
DE AltName: Full=5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate phosphatase {ECO:0000305|PubMed:27490826};
DE Short=ARPP phosphatase {ECO:0000305|PubMed:27490826};
DE Flags: Precursor;
GN Name=FHY1 {ECO:0000303|PubMed:22002057};
GN Synonyms=PYRP1 {ECO:0000303|PubMed:27490826};
GN OrderedLocusNames=At1g79790 {ECO:0000312|Araport:AT1G79790};
GN ORFNames=F20B17.21 {ECO:0000312|EMBL:AAF68115.1};
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 {ECO:0000312|EMBL:AAO42848.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [5]
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.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24123841; DOI=10.1002/cbic.201300544;
RA Haase I., Sarge S., Illarionov B., Laudert D., Hohmann H.P., Bacher A.,
RA Fischer M.;
RT "Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the
RT elusive dephosphorylation step of riboflavin biosynthesis.";
RL ChemBioChem 14:2272-2275(2013).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBSTRATE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27490826; DOI=10.1111/tpj.13291;
RA Sa N., Rawat R., Thornburg C., Walker K.D., Roje S.;
RT "Identification and characterization of the missing phosphatase on the
RT riboflavin biosynthesis pathway in Arabidopsis thaliana.";
RL Plant J. 88:705-716(2016).
CC -!- FUNCTION: FMN hydrolase that catalyzes the dephosphorylation of flavin
CC mononucleotide (FMN) to riboflavin (PubMed:22002057, PubMed:24123841,
CC PubMed:27490826). Can also dephosphorylate 5-amino-6-(5-phospho-D-
CC ribitylamino)uracil, also known as ARPP (PubMed:24123841,
CC PubMed:27490826). Not required for riboflavin biosynthesis in planta,
CC but may help maintaining flavin homeostasis within chloroplasts
CC (PubMed:27490826). {ECO:0000269|PubMed:22002057,
CC ECO:0000269|PubMed:24123841, ECO:0000269|PubMed:27490826}.
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:22002057};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + H2O = 5-amino-6-
CC (D-ribitylamino)uracil + phosphate; Xref=Rhea:RHEA:25197,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58421; EC=3.1.3.104;
CC Evidence={ECO:0000269|PubMed:24123841, ECO:0000269|PubMed:27490826};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:22002057};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.2 uM for FMN {ECO:0000269|PubMed:22002057};
CC KM=128 uM for 5-amino-6-(5-phospho-D-ribitylamino)uracil
CC {ECO:0000269|PubMed:27490826};
CC Vmax=1.42 umol/min/mg enzyme with FMN as substrate
CC {ECO:0000269|PubMed:22002057};
CC Vmax=6.73 umol/min/mg enzyme with 5-amino-6-(5-phospho-D-
CC ribitylamino)uracil as substrate {ECO:0000269|PubMed:27490826};
CC Note=kcat is 0.59 sec(-1) for FMN (PubMed:22002057). kcat is 2.80
CC sec(-1) for 5-amino-6-(5-phospho-D-ribitylamino)uracil
CC (PubMed:27490826). {ECO:0000269|PubMed:22002057,
CC ECO:0000269|PubMed:27490826};
CC pH dependence:
CC Optimum pH is 6.5-7.0 for both catalytic activities.
CC {ECO:0000269|PubMed:22002057};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius for both catalytic
CC activities. {ECO:0000269|PubMed:22002057};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27490826}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:22002057}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype and no effect on flavin
CC metabolite profile and abundances. {ECO:0000269|PubMed:27490826}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF68115.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC010793; AAF68115.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE36298.1; -; Genomic_DNA.
DR EMBL; BT004602; AAO42848.1; -; mRNA.
DR EMBL; AK227909; BAE99879.1; -; mRNA.
DR EMBL; AY086690; AAM63745.1; -; mRNA.
DR RefSeq; NP_565221.1; NM_106628.3.
DR AlphaFoldDB; Q84VZ1; -.
DR SMR; Q84VZ1; -.
DR STRING; 3702.AT1G79790.1; -.
DR PaxDb; Q84VZ1; -.
DR PRIDE; Q84VZ1; -.
DR ProteomicsDB; 230717; -.
DR EnsemblPlants; AT1G79790.1; AT1G79790.1; AT1G79790.
DR GeneID; 844318; -.
DR Gramene; AT1G79790.1; AT1G79790.1; AT1G79790.
DR KEGG; ath:AT1G79790; -.
DR Araport; AT1G79790; -.
DR TAIR; locus:2019873; AT1G79790.
DR eggNOG; KOG3085; Eukaryota.
DR HOGENOM; CLU_080554_2_0_1; -.
DR InParanoid; Q84VZ1; -.
DR OMA; YHDIPAF; -.
DR PhylomeDB; Q84VZ1; -.
DR BRENDA; 3.1.3.104; 399.
DR PRO; PR:Q84VZ1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q84VZ1; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0043726; F:5-amino-6-(5-phosphoribitylamino)uracil phosphatase activity; IEA:RHEA.
DR GO; GO:0090711; F:FMN hydrolase activity; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IDA:TAIR.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW.
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 Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Plastid; Reference proteome;
KW Riboflavin biosynthesis; Transit peptide.
FT TRANSIT 1..26
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 27..245
FT /note="Flavin mononucleotide hydrolase 1, chloroplatic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000439662"
FT CONFLICT 38
FT /note="Missing (in Ref. 5; AAM63745)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27695 MW; 66DC8F2FE728A74C CRC64;
MAAAAMHTSA EFINLKPNMW KKNPVRASGS CCLGSSSGDE ISRKRKLPIL LFDVMDTIVR
DPFYQDVPAF FGMPMKQLLE CKHPMVWIEF EKGLIDEEEL ARNFFIDGRD FDLEGLKECM
RSGYSYLDGM QELLQTLAAD DFEIHAFTNY PIWYNIIEDK LKLSAYLSWT FCSCIAGKRK
PDPEFYLEVV GHLGVEPCDC IFIDDRPTNV KCAIEIGMGG LCFENADSLA KDLSDLGINV
SVPKL
