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Reviewed, UniProtKB/Swiss-Prot O64411 (PAO_MAIZE)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Polyamine oxidase
    EC=1.5.3.n6
    EC=1.5.3.n7
    EC=1.5.3.n8
    EC=1.5.3.n9
Gene names
Name: PAO
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Zea

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Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 activity

Spermidine + O2 + H2O = 4-aminobutanal + trimethylenediamine + H2O2.

Spermine + O2 + H2O = N-(3-aminopropyl)-4-aminobutanal + trimethylenediamine + H2O2.

N(1)-acetylspermine + O2 + H2O = N-(3-acetamidopropyl)-4-aminobutanal + trimethylenediamine + H2O2.

N(8)-acetylspermidine + O2 + H2O = 4-acetamidobutanal + trimethylenediamine + H2O2.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the flavin monoamine oxidase family.

biophysicochemical properties

Kinetic parameters:

KM=38 µM for spermine

KM=40 µM for spermidine

KM=62 µM for N(1)-acetylspermine

KM=274 µM for N(1)-acetylspermidine

KM=100 µM for dioxygen

Vmax=6 µmol/min/µg enzyme with spermine as substrate

Vmax=70 µmol/min/µg enzyme with spermidine as substrate

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

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

pH dependence:

Optimum pH is 6.5.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1
Chain29 – 500472Polyamine oxidase
PRO_0000001712

Regions

Nucleotide binding42 – 432FAD
Nucleotide binding87 – 882FAD
Nucleotide binding467 – 4682FAD

Sites

Binding site631FAD
Binding site711FAD; via amide nitrogen
Binding site2651FAD; via amide nitrogen and carbonyl oxygen
Binding site4271FAD
Binding site4581FAD; via amide nitrogen

Amino acid modifications

Glycosylation1051N-linked (GlcNAc...)
Disulfide bond485 ↔ 491

Secondary structure

1 .......................................................................................... 500
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O64411-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 00BB4BAF7A2E41CB

FASTA50056,344
        10         20         30         40         50         60 
MSSSPSFGLL AVAALLLALS LAQHGSLAAT VGPRVIVVGA GMSGISAAKR LSEAGITDLL 

        70         80         90        100        110        120 
ILEATDHIGG RMHKTNFAGI NVELGANWVE GVNGGKMNPI WPIVNSTLKL RNFRSDFDYL 

       130        140        150        160        170        180 
AQNVYKEDGG VYDEDYVQKR IELADSVEEM GEKLSATLHA SGRDDMSILA MQRLNEHQPN 

       190        200        210        220        230        240 
GPATPVDMVV DYYKFDYEFA EPPRVTSLQN TVPLATFSDF GDDVYFVADQ RGYEAVVYYL 

       250        260        270        280        290        300 
AGQYLKTDDK SGKIVDPRLQ LNKVVREIKY SPGGVTVKTE DNSVYSADYV MVSASLGVLQ 

       310        320        330        340        350        360 
SDLIQFKPKL PTWKVRAIYQ FDMAVYTKIF LKFPRKFWPE GKGREFFLYA SSRRGYYGVW 

       370        380        390        400        410        420 
QEFEKQYPDA NVLLVTVTDE ESRRIEQQSD EQTKAEIMQV LRKMFPGKDV PDATDILVPR 

       430        440        450        460        470        480 
WWSDRFYKGT FSNWPVGVNR YEYDQLRAPV GRVYFTGEHT SEHYNGYVHG AYLSGIDSAE 

       490        500 
ILINCAQKKM CKYHVQGKYD

« Hide

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References

[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: 9598979] [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: 16331971] [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: 10089528] [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: 10368296] [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: 11258887] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND SYNTHETIC INHIBITORS.

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Cross-references

Sequence databases

AJ002204 mRNA. Translation: CAA05249.1.
PIRT03387.
RefSeqNP_001105106.1.
UniGeneZm.300

3D structure databases

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[»]
ModBaseSearch...

Genome annotation databases

GeneID541983.

Organism-specific databases

GrameneO64411.

Enzyme and pathway databases

BioCycMetaCyc:MON-9461.
BRENDA1.5.3.11. 289.

Family and domain databases

InterProIPR001613. Amineoxid_fl.
IPR002937. Amino_oxidase.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSPR00757. AMINEOXDASEF.
ProtoNetSearch...

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Entry information

Entry namePAO_MAIZE
AccessionPrimary (citable) accession number: O64411
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents