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Protein

Pyridoxine-5'-phosphate oxidase

Gene

Pnpo

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).By similarity

Catalytic activityi

Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2.
Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.

Cofactori

FMNNote: Binds 1 FMN per subunit.

Pathwayi: pyridoxal 5'-phosphate salvage

This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Pyridoxine-5'-phosphate oxidase (Pnpo)
This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

Pathwayi: pyridoxal 5'-phosphate salvage

This protein is involved in step 1 of the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Pyridoxine-5'-phosphate oxidase (Pnpo)
This subpathway is part of the pathway pyridoxal 5'-phosphate salvage, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxal 5'-phosphate from pyridoxine 5'-phosphate, the pathway pyridoxal 5'-phosphate salvage and in Cofactor metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001Pyridoxal 5'-phosphateBy similarity
Binding sitei139 – 1391FMNBy similarity
Binding sitei157 – 1571Pyridoxal 5'-phosphateBy similarity
Binding sitei161 – 1611Pyridoxal 5'-phosphateBy similarity
Binding sitei165 – 1651Pyridoxal 5'-phosphateBy similarity
Binding sitei219 – 2191FMNBy similarity
Binding sitei229 – 2291FMNBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi95 – 984FMNBy similarity
Nucleotide bindingi110 – 1112FMNBy similarity
Nucleotide bindingi116 – 1172FMNBy similarity
Nucleotide bindingi174 – 1752FMNBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN, Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiR-MMU-964975. Vitamins B6 activation to pyridoxal phosphate.
UniPathwayiUPA01068; UER00304.
UPA01068; UER00305.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxine-5'-phosphate oxidase (EC:1.4.3.5)
Alternative name(s):
Pyridoxamine-phosphate oxidase
Gene namesi
Name:Pnpo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2144151. Pnpo.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3271931.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Pyridoxine-5'-phosphate oxidasePRO_0000167784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei238 – 2381PhosphothreonineBy similarity
Modified residuei241 – 2411PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ91XF0.
MaxQBiQ91XF0.
PaxDbiQ91XF0.
PRIDEiQ91XF0.

PTM databases

iPTMnetiQ91XF0.
PhosphoSiteiQ91XF0.

Expressioni

Gene expression databases

BgeeiQ91XF0.
CleanExiMM_PNPO.
ExpressionAtlasiQ91XF0. baseline and differential.
GenevisibleiQ91XF0. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-1869143.
STRINGi10090.ENSMUSP00000018803.

Structurei

3D structure databases

ProteinModelPortaliQ91XF0.
SMRiQ91XF0. Positions 49-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 454Pyridoxal 5'-phosphate bindingBy similarity
Regioni225 – 2273Pyridoxal 5'-phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2586. Eukaryota.
COG0259. LUCA.
GeneTreeiENSGT00390000011219.
HOGENOMiHOG000242755.
HOVERGENiHBG045634.
InParanoidiQ91XF0.
KOiK00275.
OMAiPEHWGGY.
OrthoDBiEOG7B8S4P.
PhylomeDBiQ91XF0.
TreeFamiTF313411.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
HAMAPiMF_01629. PdxH.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERiPTHR10851:SF0. PTHR10851:SF0. 1 hit.
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00558. pdxH. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q91XF0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTCGLLSVTV TFRRPAKWTG YLRHLCCRGA VMDLGPMRKS YRGDREAFEE
60 70 80 90 100
THLTSLDPMK QFASWFDEAV QCPDIGEANA MCVATCTRDG KPSARMLLLK
110 120 130 140 150
GFGKDGFRFF TNYESRKGKE LDSNPFASLV FYWEPLNRQV RVEGPVKKLP
160 170 180 190 200
EKEAENYFHS RPKSSQIGAV VSRQSSVIPD REYLRKKNEE LGQLYQDQEV
210 220 230 240 250
PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD SPLGPMTHHG
260
EEDWVYERLA P
Length:261
Mass (Da):30,114
Last modified:December 1, 2001 - v1
Checksum:iD83A54883B4BC0EC
GO

Sequence cautioni

The sequence BAE32590.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154004 mRNA. Translation: BAE32309.1.
AK154443 mRNA. Translation: BAE32590.1. Different initiation.
AK164667 mRNA. Translation: BAE37867.1.
AL596384 Genomic DNA. Translation: CAM21902.1.
BC010785 mRNA. Translation: AAH10785.1.
BC026564 mRNA. Translation: AAH26564.1.
CCDSiCCDS25308.1.
RefSeqiNP_598782.1. NM_134021.2.
UniGeneiMm.254704.

Genome annotation databases

EnsembliENSMUST00000018803; ENSMUSP00000018803; ENSMUSG00000018659.
GeneIDi103711.
KEGGimmu:103711.
UCSCiuc007ldc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154004 mRNA. Translation: BAE32309.1.
AK154443 mRNA. Translation: BAE32590.1. Different initiation.
AK164667 mRNA. Translation: BAE37867.1.
AL596384 Genomic DNA. Translation: CAM21902.1.
BC010785 mRNA. Translation: AAH10785.1.
BC026564 mRNA. Translation: AAH26564.1.
CCDSiCCDS25308.1.
RefSeqiNP_598782.1. NM_134021.2.
UniGeneiMm.254704.

3D structure databases

ProteinModelPortaliQ91XF0.
SMRiQ91XF0. Positions 49-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1869143.
STRINGi10090.ENSMUSP00000018803.

Chemistry

ChEMBLiCHEMBL3271931.

PTM databases

iPTMnetiQ91XF0.
PhosphoSiteiQ91XF0.

Proteomic databases

EPDiQ91XF0.
MaxQBiQ91XF0.
PaxDbiQ91XF0.
PRIDEiQ91XF0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018803; ENSMUSP00000018803; ENSMUSG00000018659.
GeneIDi103711.
KEGGimmu:103711.
UCSCiuc007ldc.1. mouse.

Organism-specific databases

CTDi55163.
MGIiMGI:2144151. Pnpo.

Phylogenomic databases

eggNOGiKOG2586. Eukaryota.
COG0259. LUCA.
GeneTreeiENSGT00390000011219.
HOGENOMiHOG000242755.
HOVERGENiHBG045634.
InParanoidiQ91XF0.
KOiK00275.
OMAiPEHWGGY.
OrthoDBiEOG7B8S4P.
PhylomeDBiQ91XF0.
TreeFamiTF313411.

Enzyme and pathway databases

UniPathwayiUPA01068; UER00304.
UPA01068; UER00305.
ReactomeiR-MMU-964975. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

PROiQ91XF0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XF0.
CleanExiMM_PNPO.
ExpressionAtlasiQ91XF0. baseline and differential.
GenevisibleiQ91XF0. MM.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
HAMAPiMF_01629. PdxH.
InterProiIPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PANTHERiPTHR10851:SF0. PTHR10851:SF0. 1 hit.
PfamiPF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view]
PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
TIGRFAMsiTIGR00558. pdxH. 1 hit.
PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Stomach and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney and Liver.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 120-138, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiPNPO_MOUSE
AccessioniPrimary (citable) accession number: Q91XF0
Secondary accession number(s): Q3TP70, Q3U445, Q3U4X1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: December 1, 2001
Last modified: June 8, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.