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Protein

Polyamine oxidase

Gene

PAO

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

FADNote: 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. N1-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
  2. N1-acetylspermine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
  3. N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
  4. spermidine oxidase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
  5. spermine oxidase (propane-1,3-diamine-forming) activity Source: UniProtKB-EC
Complete GO annotation...

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
ProteomesiUP000007305: Unplaced

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MSSSPSFGLL AVAALLLALS LAQHGSLAAT VGPRVIVVGA GMSGISAAKR
60 70 80 90 100
LSEAGITDLL ILEATDHIGG RMHKTNFAGI NVELGANWVE GVNGGKMNPI
110 120 130 140 150
WPIVNSTLKL RNFRSDFDYL AQNVYKEDGG VYDEDYVQKR IELADSVEEM
160 170 180 190 200
GEKLSATLHA SGRDDMSILA MQRLNEHQPN GPATPVDMVV DYYKFDYEFA
210 220 230 240 250
EPPRVTSLQN TVPLATFSDF GDDVYFVADQ RGYEAVVYYL AGQYLKTDDK
260 270 280 290 300
SGKIVDPRLQ LNKVVREIKY SPGGVTVKTE DNSVYSADYV MVSASLGVLQ
310 320 330 340 350
SDLIQFKPKL PTWKVRAIYQ FDMAVYTKIF LKFPRKFWPE GKGREFFLYA
360 370 380 390 400
SSRRGYYGVW QEFEKQYPDA NVLLVTVTDE ESRRIEQQSD EQTKAEIMQV
410 420 430 440 450
LRKMFPGKDV PDATDILVPR WWSDRFYKGT FSNWPVGVNR YEYDQLRAPV
460 470 480 490 500
GRVYFTGEHT SEHYNGYVHG AYLSGIDSAE ILINCAQKKM CKYHVQGKYD
Length:500
Mass (Da):56,344
Last modified:August 1, 1998 - v1
Checksum:i00BB4BAF7A2E41CB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002204 mRNA. Translation: CAA05249.1.
PIRiT03387.
RefSeqiNP_001105106.1. NM_001111636.1.
UniGeneiZm.300.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Chemistry

BindingDBiO64411.
ChEMBLiCHEMBL6108.

Protein family/group databases

Allergomei955. Zea m PAO.

Proteomic databases

PRIDEiO64411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi541983.
KEGGizma:541983.

Organism-specific databases

GrameneiO64411.

Phylogenomic databases

HOGENOMiHOG000174927.
KOiK13366.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9461.
SABIO-RKO64411.

Miscellaneous databases

EvolutionaryTraceiO64411.

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.
ProtoNetiSearch...

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: February 4, 2015
This is version 103 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, Complete proteome, Direct protein sequencing, Reference proteome

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

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.