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Q91XF0

- PNPO_MOUSE

UniProt

Q91XF0 - PNPO_MOUSE

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Protein

Pyridoxine-5'-phosphate oxidase

Gene

Pnpo

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

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: UniProtKB-EC

GO - Biological processi

  1. 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: Ensembl
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.
OMAiNMGSRKA.
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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25308.1.
RefSeqi NP_598782.1. NM_134021.2.
UniGenei Mm.254704.

3D structure databases

ProteinModelPortali Q91XF0.
SMRi Q91XF0. Positions 49-261.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1869143.
STRINGi 10090.ENSMUSP00000018803.

PTM databases

PhosphoSitei Q91XF0.

Proteomic databases

MaxQBi Q91XF0.
PaxDbi Q91XF0.
PRIDEi Q91XF0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018803 ; ENSMUSP00000018803 ; ENSMUSG00000018659 .
GeneIDi 103711.
KEGGi mmu:103711.
UCSCi uc007ldc.1. mouse.

Organism-specific databases

CTDi 55163.
MGIi MGI:2144151. Pnpo.

Phylogenomic databases

eggNOGi COG0259.
GeneTreei ENSGT00390000011219.
HOGENOMi HOG000242755.
HOVERGENi HBG045634.
InParanoidi Q91XF0.
KOi K00275.
OMAi NMGSRKA.
OrthoDBi EOG7B8S4P.
PhylomeDBi Q91XF0.
TreeFami TF313411.

Enzyme and pathway databases

UniPathwayi UPA00190 ; UER00304 .
UPA00190 ; UER00305 .
Reactomei REACT_198547. Vitamins B6 activation to pyridoxal phosphate.

Miscellaneous databases

NextBioi 356069.
PROi Q91XF0.
SOURCEi Search...

Gene expression databases

Bgeei Q91XF0.
CleanExi MM_PNPO.
ExpressionAtlasi Q91XF0. baseline and differential.
Genevestigatori Q91XF0.

Family and domain databases

Gene3Di 2.30.110.10. 1 hit.
HAMAPi MF_01629. PdxH.
InterProi IPR000659. Pyridox_Oxase.
IPR019740. Pyridox_Oxase_CS.
IPR011576. Pyridox_Oxase_FMN-bd.
IPR019576. Pyridoxamine_oxidase_dimer_C.
IPR012349. Split_barrel_FMN-bd.
[Graphical view ]
PANTHERi PTHR10851. PTHR10851. 1 hit.
Pfami PF10590. PNPOx_C. 1 hit.
PF01243. Pyridox_oxidase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
SUPFAMi SSF50475. SSF50475. 1 hit.
TIGRFAMsi TIGR00558. pdxH. 1 hit.
PROSITEi PS01064. PYRIDOX_OXIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 108 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