PNPO_BOMMO
ID PNPO_BOMMO Reviewed; 257 AA.
AC Q1PCB0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000305};
DE EC=1.4.3.5 {ECO:0000269|PubMed:19523068};
DE AltName: Full=BmPNPO {ECO:0000303|PubMed:27106120};
DE AltName: Full=PNP/PMP oxidase {ECO:0000305};
DE Short=PNPOx {ECO:0000305};
DE AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000305};
GN Name=PNPO {ECO:0000303|PubMed:19523068, ECO:0000303|PubMed:27106120,
GN ECO:0000312|EMBL:ABE28379.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000312|EMBL:ABE28379.1};
RN [1] {ECO:0000312|EMBL:ABE28379.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DEVELOPMENTAL STAGE, AND
RP 3D-STRUCTURE MODELING.
RC TISSUE=Fat body {ECO:0000312|EMBL:ABE28379.1};
RX PubMed=19523068; DOI=10.1111/j.1365-2583.2009.00880.x;
RA Huang S.H., Shi R.J., Zhang J.Y., Wang Z., Huang L.Q.;
RT "Cloning and characterization of a pyridoxine 5'-phosphate oxidase from
RT silkworm, Bombyx mori.";
RL Insect Mol. Biol. 18:365-371(2009).
RN [2] {ECO:0000312|EnsemblMetazoa:BGIBMGA005391-TA}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000312|EnsemblMetazoa:BGIBMGA005391-TA};
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [3]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=26780217; DOI=10.1016/j.cbpb.2016.01.002;
RA Huang S., Yang H., Yao L., Zhang J., Huang L.;
RT "Effect of exogenous hormones on transcription levels of pyridoxal 5'-
RT phosphate biosynthetic enzymes in the silkworm (Bombyx mori).";
RL Comp. Biochem. Physiol. 194:20-24(2016).
RN [4]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27106120; DOI=10.1016/j.gene.2016.04.035;
RA Huang S., Yao L., Zhang J., Huang L.;
RT "Direct and indirect effects of RNA interference against pyridoxal kinase
RT and pyridoxine 5'-phosphate oxidase genes in Bombyx mori.";
RL Gene 587:48-52(2016).
CC -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-phosphate
CC (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate
CC (PLP). {ECO:0000269|PubMed:19523068}.
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|PubMed:19523068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15818;
CC Evidence={ECO:0000305|PubMed:19523068};
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|PubMed:19523068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15150;
CC Evidence={ECO:0000305|PubMed:19523068};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q9NVS9};
CC Note=Binds 1 FMN per subunit. {ECO:0000250|UniProtKB:Q9NVS9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.15 uM for pyridoxamine 5'-phosphate (at pH 9.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:19523068};
CC KM=0.65 uM for pyridoxine 5'-phosphate (at pH 9.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:19523068};
CC pH dependence:
CC Optimum pH is 9.0. Active between pH 7.0 and 10.5.
CC {ECO:0000269|PubMed:19523068};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC {ECO:0000305|PubMed:19523068}.
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC {ECO:0000305|PubMed:19523068}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19523068}.
CC -!- TISSUE SPECIFICITY: Expressed in silk gland and fat body of the larva.
CC {ECO:0000269|PubMed:26780217}.
CC -!- DEVELOPMENTAL STAGE: Expressed in fifth instar larva (PubMed:19523068,
CC PubMed:26780217, PubMed:27106120). In the silk gland, highest level on
CC the first day of 5th instar larva, then displaying a decreasing trend
CC daily. In the fat body, expression level is high in the early and late
CC stages, and low in the middle stage of 5th instar larva
CC (PubMed:26780217). {ECO:0000269|PubMed:19523068,
CC ECO:0000269|PubMed:26780217, ECO:0000269|PubMed:27106120}.
CC -!- INDUCTION: Expression is up-regulated by exogenous molting hormone
CC (beta-ecdysterone) and down-regulated by exogenous juvenile hormone
CC (JH) III in the silk gland and fat body of the fifth instar larva.
CC {ECO:0000269|PubMed:26780217}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown of this protein causes
CC significant decrease in transcription levels of pyridoxal 5'-phosphate
CC (PLP)-dependent enzymes phosphoserine aminotransferase (PSAT) and
CC aspartate aminotransferase (glutamic-oxaloacetic transaminase) in silk
CC gland, fat body and midgut of the fifth instar larva.
CC {ECO:0000269|PubMed:27106120}.
CC -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase family.
CC {ECO:0000305}.
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DR EMBL; DQ452398; ABE28379.1; -; mRNA.
DR EMBL; BABH01013608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001037442.1; NM_001043977.1.
DR AlphaFoldDB; Q1PCB0; -.
DR SMR; Q1PCB0; -.
DR STRING; 7091.BGIBMGA005391-TA; -.
DR EnsemblMetazoa; BGIBMGA005391-RA; BGIBMGA005391-TA; BGIBMGA005391.
DR GeneID; 693010; -.
DR KEGG; bmor:693010; -.
DR CTD; 55163; -.
DR eggNOG; KOG2586; Eukaryota.
DR HOGENOM; CLU_032263_2_1_1; -.
DR InParanoid; Q1PCB0; -.
DR OMA; PEPNAMV; -.
DR OrthoDB; 1337072at2759; -.
DR BRENDA; 1.4.3.5; 890.
DR UniPathway; UPA01068; UER00304.
DR UniPathway; UPA01068; UER00305.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IDA:UniProtKB.
DR GO; GO:0002168; P:instar larval development; IEP:UniProtKB.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008614; P:pyridoxine metabolic process; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IEP:UniProtKB.
DR Gene3D; 2.30.110.10; -; 1.
DR HAMAP; MF_01629; PdxH; 1.
DR InterPro; IPR000659; Pyridox_Oxase.
DR InterPro; IPR019740; Pyridox_Oxase_CS.
DR InterPro; IPR011576; Pyridox_Oxase_put.
DR InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR PANTHER; PTHR10851; PTHR10851; 1.
DR Pfam; PF10590; PNP_phzG_C; 1.
DR Pfam; PF01243; Putative_PNPOx; 1.
DR PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR TIGRFAMs; TIGR00558; pdxH; 1.
DR PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE 1: Evidence at protein level;
KW Flavoprotein; FMN; Oxidoreductase; Pyridoxal phosphate;
KW Pyridoxine biosynthesis; Reference proteome.
FT CHAIN 1..257
FT /note="Pyridoxine/pyridoxamine 5'-phosphate oxidase"
FT /id="PRO_0000451715"
FT BINDING 33..36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 90..93
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 95
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 105..106
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 112
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 152
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 156
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 160
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 169..170
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q9NVS9"
FT BINDING 216
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 222..224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
FT BINDING 226
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:P0AFI7"
SQ SEQUENCE 257 AA; 29865 MW; 3E3FC64256048204 CRC64;
MLNNCVVLIR KSVLLSPNLK YIRNMSIDIG GMRIKYKEKD ETFLEKHLVS KEPFGQFKSW
FEEACARKEI LEPNAMCLAT VSQEGFPSAR FVLCKGYGKE GFKFYTNYGS KKAKDIEGNP
NVAATFYWEI LNRSVRIEGR VEKLSEDDST KYFHTRPVVS QIAACASYQS TPIESRDVLC
EREKLLEQQY MIPGKEVPKP SYWGGYLLIP RSVEFWQGQR DRLHDRIKFR RPNKGEVSDE
RLLHEGEDGW VFERLSP
