PPOX2_ARATH
ID PPOX2_ARATH Reviewed; 198 AA.
AC Q9ZPY1;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase 2;
DE Short=AtPPOX1;
DE EC=1.4.3.5;
GN Name=PPOX2; OrderedLocusNames=At2g46580; ORFNames=F13A10.11;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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.
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX DOI=10.1007/s11738-010-0579-6;
RA Sang Y., Goertzen L.R., Tzou Y.-M., Locy R.D., Singh N.K.;
RT "Identification of a second pyridoxine (pyridoxamine) 50-phosphate oxidase
RT in Arabidopsis thaliana.";
RL Acta Physiol. Plant. 33:559-566(2011).
CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate
CC (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC (PLP). Has an in vitro catalytic efficiency for PNP approximately 300-
CC fold lower than that of PPOX1. {ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) +
CC pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC Evidence={ECO:0000269|Ref.5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-phosphate;
CC Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58589, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC Evidence={ECO:0000269|Ref.5};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; AC006418; AAD20168.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC10724.1; -; Genomic_DNA.
DR EMBL; AY086412; AAM63414.1; -; mRNA.
DR EMBL; BT024917; ABD94073.1; -; mRNA.
DR PIR; F84904; F84904.
DR RefSeq; NP_566081.1; NM_130223.3.
DR AlphaFoldDB; Q9ZPY1; -.
DR SMR; Q9ZPY1; -.
DR STRING; 3702.AT2G46580.1; -.
DR iPTMnet; Q9ZPY1; -.
DR PaxDb; Q9ZPY1; -.
DR PRIDE; Q9ZPY1; -.
DR ProteomicsDB; 236650; -.
DR EnsemblPlants; AT2G46580.1; AT2G46580.1; AT2G46580.
DR GeneID; 819270; -.
DR Gramene; AT2G46580.1; AT2G46580.1; AT2G46580.
DR KEGG; ath:AT2G46580; -.
DR Araport; AT2G46580; -.
DR TAIR; locus:2039949; AT2G46580.
DR eggNOG; KOG4558; Eukaryota.
DR HOGENOM; CLU_058669_1_2_1; -.
DR OMA; ARLQFAW; -.
DR OrthoDB; 1531309at2759; -.
DR PhylomeDB; Q9ZPY1; -.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR PRO; PR:Q9ZPY1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPY1; baseline and differential.
DR Genevisible; Q9ZPY1; AT.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IDA:UniProtKB.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IDA:UniProtKB.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR000659; Pyridox_Oxase.
DR InterPro; IPR024624; Pyridox_Oxase_Alr4036_FMN-bd.
DR InterPro; IPR024015; Pyridox_Oxase_FMN-dep_Alr4036.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR10851; PTHR10851; 1.
DR Pfam; PF12766; Pyridox_oxase_2; 1.
DR TIGRFAMs; TIGR04026; PPOX_FMN_cyano; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Oxidoreductase; Pyridoxine biosynthesis;
KW Reference proteome.
FT CHAIN 1..198
FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase 2"
FT /id="PRO_0000420550"
FT BINDING 42
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 59..60
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 121..122
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
SQ SEQUENCE 198 AA; 22620 MW; EFDE8DA20D6A4376 CRC64;
MGTHVAPWKQ LLFGAIEANS HLSHSSYVQL ATIGLNGRPS NRTVVFRGFE ENSDRIQINT
DLRSRKIEEL KHCPFSEMCW YFSDTWEQFR INGRIEVIDA SNPDQTKLQQ REKAWFANSL
RSRLIYVCPT PGSPCNSEQS SQQVKLDPSS GPVPEYCLLL LEPEKVDYLN LKTNQRLFFS
SMATGTGEKC WTSEKVNP
