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O64411

- PAO_MAIZE

UniProt

O64411 - PAO_MAIZE

Protein

Polyamine oxidase

Gene

PAO

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of the secondary amino group of polyamines (spermine, spermidine and their acetyl derivatives). Plays an important role in the regulation of polyamine intracellular concentration.

    Catalytic activityi

    Spermidine + O2 + H2O = propane-1,3-diamine + 4-aminobutanal +H2O2.
    N(8)-acetylspermidine + O2 + H2O = propane-1,3-diamine + 4-acetamidobutanal + H2O2.
    Spermine + O2 + H2O = N-(3-aminopropyl)-4-aminobutanal + trimethylenediamine + H2O2.
    N(1)-acetylspermine + O2 + H2O = N-(3-acetamidopropyl)-4-aminobutanal + trimethylenediamine + H2O2.

    Cofactori

    Binds 1 FAD per subunit.

    Kineticsi

    1. KM=38 µM for spermine2 Publications
    2. KM=40 µM for spermidine2 Publications
    3. KM=62 µM for N(1)-acetylspermine2 Publications
    4. KM=274 µM for N(1)-acetylspermidine2 Publications
    5. KM=100 µM for dioxygen2 Publications

    Vmax=6 µmol/min/µg enzyme with spermine as substrate2 Publications

    Vmax=70 µmol/min/µg enzyme with spermidine as substrate2 Publications

    Vmax=21 µmol/min/µg enzyme with N(1)-acetylspermine as substrate2 Publications

    Vmax=2.5 µmol/min/µg enzyme with N(1)-acetylspermidine as substrate2 Publications

    pH dependencei

    Optimum pH is 6.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei63 – 631FAD
    Binding sitei71 – 711FAD; via amide nitrogen
    Binding sitei265 – 2651FAD; via amide nitrogen and carbonyl oxygen
    Binding sitei427 – 4271FAD
    Binding sitei458 – 4581FAD; via amide nitrogen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi42 – 432FAD
    Nucleotide bindingi87 – 882FAD
    Nucleotide bindingi467 – 4682FAD

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: EnsemblPlants/Gramene
    2. N1-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
    3. N1-acetylspermine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
    4. N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
    5. polyamine oxidase activity Source: EnsemblPlants/Gramene
    6. spermidine oxidase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
    7. spermine oxidase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC

    GO - Biological processi

    1. polyamine catabolic process Source: EnsemblPlants/Gramene

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-9461.
    SABIO-RKO64411.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyamine oxidase (EC:1.5.3.14, EC:1.5.3.15)
    Gene namesi
    Name:PAO
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

    Organism-specific databases

    GrameneiO64411.

    Pathology & Biotechi

    Protein family/group databases

    Allergomei955. Zea m PAO.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28281 PublicationAdd
    BLAST
    Chaini29 – 500472Polyamine oxidasePRO_0000001712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi105 – 1051N-linked (GlcNAc...)
    Disulfide bondi485 ↔ 491

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiO64411.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 384
    Helixi42 – 5312
    Beta strandi59 – 624
    Beta strandi64 – 696
    Beta strandi74 – 774
    Beta strandi80 – 856
    Beta strandi88 – 969
    Helixi100 – 1056
    Beta strandi112 – 1143
    Helixi120 – 1223
    Beta strandi124 – 1263
    Beta strandi127 – 1315
    Helixi134 – 15623
    Helixi168 – 1769
    Beta strandi178 – 1814
    Helixi185 – 19410
    Helixi196 – 1994
    Turni203 – 2053
    Beta strandi206 – 2083
    Turni209 – 2113
    Helixi215 – 2206
    Beta strandi222 – 2276
    Helixi235 – 2428
    Turni249 – 2513
    Beta strandi259 – 2624
    Beta strandi265 – 2706
    Beta strandi275 – 2795
    Beta strandi284 – 2929
    Helixi296 – 3005
    Beta strandi303 – 3086
    Helixi312 – 3209
    Beta strandi321 – 3244
    Beta strandi326 – 3327
    Beta strandi345 – 3495
    Beta strandi352 – 3576
    Beta strandi359 – 3624
    Turni364 – 3663
    Beta strandi367 – 3693
    Beta strandi372 – 3787
    Helixi379 – 3868
    Helixi390 – 40415
    Beta strandi406 – 4083
    Beta strandi414 – 4174
    Turni421 – 4233
    Turni425 – 4273
    Beta strandi428 – 4336
    Helixi440 – 4478
    Beta strandi453 – 4553
    Helixi458 – 4603
    Turni462 – 4665
    Helixi468 – 48821

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B37X-ray1.90A/B/C29-500[»]
    1B5QX-ray1.90A/B/C29-500[»]
    1H81X-ray2.10A/B/C29-500[»]
    1H82X-ray1.90A/B/C29-500[»]
    1H83X-ray1.90A/B/C29-500[»]
    1H84X-ray2.00A/B/C29-500[»]
    1H86X-ray2.00A/B/C29-500[»]
    3KPFX-ray2.90A/B29-500[»]
    3KU9X-ray3.20A/B29-500[»]
    3L1RX-ray3.20A/B29-500[»]
    ProteinModelPortaliO64411.
    SMRiO64411. Positions 33-494.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO64411.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the flavin monoamine oxidase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000174927.
    KOiK13366.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00757. AMINEOXDASEF.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O64411-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSPSFGLL AVAALLLALS LAQHGSLAAT VGPRVIVVGA GMSGISAAKR    50
    LSEAGITDLL ILEATDHIGG RMHKTNFAGI NVELGANWVE GVNGGKMNPI 100
    WPIVNSTLKL RNFRSDFDYL AQNVYKEDGG VYDEDYVQKR IELADSVEEM 150
    GEKLSATLHA SGRDDMSILA MQRLNEHQPN GPATPVDMVV DYYKFDYEFA 200
    EPPRVTSLQN TVPLATFSDF GDDVYFVADQ RGYEAVVYYL AGQYLKTDDK 250
    SGKIVDPRLQ LNKVVREIKY SPGGVTVKTE DNSVYSADYV MVSASLGVLQ 300
    SDLIQFKPKL PTWKVRAIYQ FDMAVYTKIF LKFPRKFWPE GKGREFFLYA 350
    SSRRGYYGVW QEFEKQYPDA NVLLVTVTDE ESRRIEQQSD EQTKAEIMQV 400
    LRKMFPGKDV PDATDILVPR WWSDRFYKGT FSNWPVGVNR YEYDQLRAPV 450
    GRVYFTGEHT SEHYNGYVHG AYLSGIDSAE ILINCAQKKM CKYHVQGKYD 500
    Length:500
    Mass (Da):56,344
    Last modified:August 1, 1998 - v1
    Checksum:i00BB4BAF7A2E41CB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002204 mRNA. Translation: CAA05249.1.
    PIRiT03387.
    RefSeqiNP_001105106.1. NM_001111636.1.
    UniGeneiZm.300.

    Genome annotation databases

    GeneIDi541983.
    KEGGizma:541983.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002204 mRNA. Translation: CAA05249.1 .
    PIRi T03387.
    RefSeqi NP_001105106.1. NM_001111636.1.
    UniGenei Zm.300.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B37 X-ray 1.90 A/B/C 29-500 [» ]
    1B5Q X-ray 1.90 A/B/C 29-500 [» ]
    1H81 X-ray 2.10 A/B/C 29-500 [» ]
    1H82 X-ray 1.90 A/B/C 29-500 [» ]
    1H83 X-ray 1.90 A/B/C 29-500 [» ]
    1H84 X-ray 2.00 A/B/C 29-500 [» ]
    1H86 X-ray 2.00 A/B/C 29-500 [» ]
    3KPF X-ray 2.90 A/B 29-500 [» ]
    3KU9 X-ray 3.20 A/B 29-500 [» ]
    3L1R X-ray 3.20 A/B 29-500 [» ]
    ProteinModelPortali O64411.
    SMRi O64411. Positions 33-494.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi O64411.
    ChEMBLi CHEMBL6108.

    Protein family/group databases

    Allergomei 955. Zea m PAO.

    Proteomic databases

    PRIDEi O64411.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 541983.
    KEGGi zma:541983.

    Organism-specific databases

    Gramenei O64411.

    Phylogenomic databases

    HOGENOMi HOG000174927.
    KOi K13366.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-9461.
    SABIO-RK O64411.

    Miscellaneous databases

    EvolutionaryTracei O64411.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002937. Amino_oxidase.
    IPR001613. Flavin_amine_oxidase.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    PRINTSi PR00757. AMINEOXDASEF.
    ProtoNeti Search...

    Publicationsi

    1. "Maize polyamine oxidase: primary structure from protein and cDNA sequencing."
      Tavladoraki P., Schinina M.E., Cecconi F., Di Agostino S., Manera F., Rea G., Mariottini P., Federico R., Angelini R.
      FEBS Lett. 426:62-66(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 29-93; 97-111; 115-147; 150-152; 154-162; 164-225; 227-241; 254-266; 270-278; 292-314; 317-323; 329-332; 343-352; 355-383; 385-394; 404-459; 461-471; 477-487 AND 493-496.
      Strain: cv. Paolo.
      Tissue: Etiolated seedling.
    2. "Properties of the polyamine oxidase from the cell wall of maize seedlings."
      Federico R., Alisi C., Forlani F.
      Phytochemistry 28:45-46(1989)
      Cited for: SUBSTRATE SPECIFICITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "Oxidation of acetylpolyamines by maize polyamine oxidase."
      Federico R., Ercolini L., Laurenzi M., Angelini R.
      Phytochemistry 43:339-341(1996)
      Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    4. "Lys300 plays a major role in the catalytic mechanism of maize polyamine oxidase."
      Polticelli F., Basran J., Faso C., Cona A., Minervini G., Angelini R., Federico R., Scrutton N.S., Tavladoraki P.
      Biochemistry 44:16108-16120(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REACTION MECHANISM.
    5. "Crystallization and preliminary X-ray analysis of polyamine oxidase from Zea mays L."
      Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.
      Acta Crystallogr. D 54:1429-1431(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), CRYSTALLIZATION.
    6. "A 30-A-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase."
      Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.
      Structure 7:265-276(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND SYNTHETIC INHIBITOR.
    7. "Structural bases for inhibitor binding and catalysis in polyamine oxidase."
      Binda C., Angelini R., Federico R., Ascenzi P., Mattevi A.
      Biochemistry 40:2766-2776(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND SYNTHETIC INHIBITORS.

    Entry informationi

    Entry nameiPAO_MAIZE
    AccessioniPrimary (citable) accession number: O64411
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 99 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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3