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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951FMNBy similarity
Binding sitei98 – 981FMN; via amide nitrogenBy similarity
Binding sitei100 – 1001SubstrateBy similarity
Binding sitei117 – 1171FMNBy similarity
Binding sitei157 – 1571SubstrateBy similarity
Binding sitei161 – 1611SubstrateBy similarity
Binding sitei165 – 1651SubstrateBy similarity

Regions

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

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. pyridoxamine-phosphate oxidase activity Source: GO_Central

GO - Biological processi

  1. pyridoxal phosphate biosynthetic process Source: GO_Central
  2. pyridoxine biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridoxine biosynthesis

Keywords - Ligandi

Flavoprotein, FMN, Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_198547. Vitamins B6 activation to pyridoxal phosphate.
UniPathwayiUPA00190; UER00304.
UPA00190; 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
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:2144151. Pnpo.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ91XF0.
PaxDbiQ91XF0.
PRIDEiQ91XF0.

PTM databases

PhosphoSiteiQ91XF0.

Expressioni

Gene expression databases

BgeeiQ91XF0.
CleanExiMM_PNPO.
ExpressionAtlasiQ91XF0. baseline and differential.
GenevestigatoriQ91XF0.

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
Regioni225 – 2273Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0259.
GeneTreeiENSGT00390000011219.
HOGENOMiHOG000242755.
HOVERGENiHBG045634.
InParanoidiQ91XF0.
KOiK00275.
OMAiPHWGGFR.
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. PTHR10851. 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.

PTM databases

PhosphoSiteiQ91XF0.

Proteomic databases

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

eggNOGiCOG0259.
GeneTreeiENSGT00390000011219.
HOGENOMiHOG000242755.
HOVERGENiHBG045634.
InParanoidiQ91XF0.
KOiK00275.
OMAiPHWGGFR.
OrthoDBiEOG7B8S4P.
PhylomeDBiQ91XF0.
TreeFamiTF313411.

Enzyme and pathway databases

UniPathwayiUPA00190; UER00304.
UPA00190; UER00305.
ReactomeiREACT_198547. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

NextBioi356069.
PROiQ91XF0.
SOURCEiSearch...

Gene expression databases

BgeeiQ91XF0.
CleanExiMM_PNPO.
ExpressionAtlasiQ91XF0. baseline and differential.
GenevestigatoriQ91XF0.

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. PTHR10851. 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.

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: February 4, 2015
This is version 111 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

External Data

Dasty 3

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 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.