Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable polyamine oxidase 4

Gene

PAO4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Flavoenzyme that catalyzes the oxidation of the secondary amino group of spermine. No activity detected when spermidine, putrescine or N(1)-acetylspermine are used as substrates.

Catalytic activityi

Spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2.1 Publication

Cofactori

FADBy similarityNote: Binds 1 FAD per subunit.By similarity

Kineticsi

  1. KM=0.23 mM for spermine1 Publication

    pH dependencei

    Optimum pH is 7.5-8.5.1 Publication

    GO - Molecular functioni

    GO - Biological processi

    • polyamine catabolic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciARA:AT1G65840-MONOMER.
    MetaCyc:AT1G65840-MONOMER.
    BRENDAi1.5.3.16. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable polyamine oxidase 4 (EC:1.5.3.16)
    Short name:
    AtPAO4
    Alternative name(s):
    Amine oxidase 2
    Gene namesi
    Name:PAO4
    Ordered Locus Names:At1g65840
    ORF Names:F1E22.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G65840.

    Subcellular locationi

    GO - Cellular componenti

    • peroxisome Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 497497Probable polyamine oxidase 4PRO_0000352510Add
    BLAST

    Proteomic databases

    PaxDbiQ8H191.
    PRIDEiQ8H191.

    Expressioni

    Tissue specificityi

    Highly expressed in roots, flowers and greening cotelydons. Lower expression in other tissues.1 Publication

    Inductioni

    By abscisic acid, salicylic acid, wounding and flagellin 22, a pathogen elicitor.1 Publication

    Gene expression databases

    GenevisibleiQ8H191. AT.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT1G65840.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8H191.
    SMRiQ8H191. Positions 29-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family.Curated

    Phylogenomic databases

    eggNOGiKOG0029. Eukaryota.
    ENOG410XSNC. LUCA.
    HOGENOMiHOG000037651.
    InParanoidiQ8H191.
    KOiK17839.
    OMAiGARWLHN.
    PhylomeDBiQ8H191.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    IPR001613. Flavin_amine_oxidase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.
    SUPFAMiSSF51905. SSF51905. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q8H191-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDKKKNSFPD NLPEGTISEL MQKQNNVQPS VIVIGSGISG LAAARNLSEA
    60 70 80 90 100
    SFKVTVLESR DRIGGRIHTD YSFGCPVDMG ASWLHGVSDE NPLAPIIRRL
    110 120 130 140 150
    GLTLYRTSGD DSILYDHDLE SYGLFDMHGN KIPPQLVTKV GDAFKRILEE
    160 170 180 190 200
    TEKIRDETAN DMSVLQGISI VLDRNPELRQ EGMAYEVLQW YLCRMEAWFA
    210 220 230 240 250
    VDANLISLKC WDQDECLSGG HGLMVQGYEP VIRTIAKDLD IRLNHRVTKV
    260 270 280 290 300
    VRTSNNKVIV AVEGGTNFVA DAVIITVPIG VLKANLIQFE PELPQWKTSA
    310 320 330 340 350
    ISGLGVGNEN KIALRFDRAF WPNVEFLGMV APTSYACGYF LNLHKATGHP
    360 370 380 390 400
    VLVYMAAGNL AQDLEKLSDE ATANFVMLQL KKMFPDAPDP AQYLVTRWGT
    410 420 430 440 450
    DPNTLGCYAY DVVGMPEDLY PRLGEPVDNI FFGGEAVNVE HQGSAHGAFL
    460 470 480 490
    AGVSASQNCQ RYIFERLGAW EKLKLVSLMG NSDILETATV PLQISRM
    Length:497
    Mass (Da):54,931
    Last modified:March 1, 2003 - v1
    Checksum:i69CEE30B841B022C
    GO

    Sequence cautioni

    The sequence AAF23834.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti283 – 2831K → R in AAK43885 (PubMed:14593172).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF364953 mRNA. Translation: AAO85405.1.
    AC007234 Genomic DNA. Translation: AAF23834.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE34430.1.
    AF370508 mRNA. Translation: AAK43885.1.
    BT000353 mRNA. Translation: AAN15672.1.
    PIRiD96682.
    RefSeqiNP_176759.1. NM_105256.3.
    UniGeneiAt.16379.

    Genome annotation databases

    EnsemblPlantsiAT1G65840.1; AT1G65840.1; AT1G65840.
    GeneIDi842894.
    GrameneiAT1G65840.1; AT1G65840.1; AT1G65840.
    KEGGiath:AT1G65840.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF364953 mRNA. Translation: AAO85405.1.
    AC007234 Genomic DNA. Translation: AAF23834.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE34430.1.
    AF370508 mRNA. Translation: AAK43885.1.
    BT000353 mRNA. Translation: AAN15672.1.
    PIRiD96682.
    RefSeqiNP_176759.1. NM_105256.3.
    UniGeneiAt.16379.

    3D structure databases

    ProteinModelPortaliQ8H191.
    SMRiQ8H191. Positions 29-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT1G65840.1.

    Proteomic databases

    PaxDbiQ8H191.
    PRIDEiQ8H191.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G65840.1; AT1G65840.1; AT1G65840.
    GeneIDi842894.
    GrameneiAT1G65840.1; AT1G65840.1; AT1G65840.
    KEGGiath:AT1G65840.

    Organism-specific databases

    TAIRiAT1G65840.

    Phylogenomic databases

    eggNOGiKOG0029. Eukaryota.
    ENOG410XSNC. LUCA.
    HOGENOMiHOG000037651.
    InParanoidiQ8H191.
    KOiK17839.
    OMAiGARWLHN.
    PhylomeDBiQ8H191.

    Enzyme and pathway databases

    BioCyciARA:AT1G65840-MONOMER.
    MetaCyc:AT1G65840-MONOMER.
    BRENDAi1.5.3.16. 399.

    Miscellaneous databases

    PROiQ8H191.

    Gene expression databases

    GenevisibleiQ8H191. AT.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR023753. FAD/NAD-binding_dom.
    IPR001613. Flavin_amine_oxidase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.
    SUPFAMiSSF51905. SSF51905. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "A putative amine oxidase 2 from Arabidopsis."
      Pinontoan R., Cunningham K.W., Iida H., Uozumi N., Muto S.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Landsberg erecta.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Heterologous expression and biochemical characterization of a polyamine oxidase from Arabidopsis involved in polyamine back conversion."
      Tavladoraki P., Rossi M.N., Saccuti G., Perez-Amador M.A., Polticelli F., Angelini R., Federico R.
      Plant Physiol. 141:1519-1532(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    6. "A putative peroxisomal polyamine oxidase, AtPAO4, is involved in polyamine catabolism in Arabidopsis thaliana."
      Kamada-Nobusada T., Hayashi M., Fukazawa M., Sakakibara H., Nishimura M.
      Plant Cell Physiol. 49:1272-1282(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.
    7. "Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis thaliana."
      Moschou P.N., Sanmartin M., Andriopoulou A.H., Rojo E., Sanchez-Serrano J.J., Roubelakis-Angelakis K.A.
      Plant Physiol. 147:1845-1857(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiPAO4_ARATH
    AccessioniPrimary (citable) accession number: Q8H191
    Secondary accession number(s): Q94JZ7, Q9SHX4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 14, 2008
    Last sequence update: March 1, 2003
    Last modified: February 17, 2016
    This is version 94 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. 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.