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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
  1. Vmax=6 µmol/min/µg enzyme with spermine as substrate2 Publications
  2. Vmax=70 µmol/min/µg enzyme with spermidine as substrate2 Publications
  3. Vmax=21 µmol/min/µg enzyme with N(1)-acetylspermine as substrate2 Publications
  4. 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)DescriptionActionsGraphical viewLength
Binding sitei63FAD1
Binding sitei71FAD; via amide nitrogen1
Binding sitei265FAD; via amide nitrogen and carbonyl oxygen1
Binding sitei427FAD1
Binding sitei458FAD; via amide nitrogen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 43FAD2
Nucleotide bindingi87 – 88FAD2
Nucleotide bindingi467 – 468FAD2

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9461.
BRENDAi1.5.3.14. 6752.
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 cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
Proteomesi
  • UP000007305 Componenti: Unplaced

Pathology & Biotechi

Protein family/group databases

Allergomei955. Zea m PAO.

Chemistry databases

ChEMBLiCHEMBL6108.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 281 PublicationAdd BLAST28
ChainiPRO_000000171229 – 500Polyamine oxidaseAdd BLAST472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi105N-linked (GlcNAc...)1
Disulfide bondi485 ↔ 491

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO64411.
PRIDEiO64411.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi4577.GRMZM2G034152_P01.

Chemistry databases

BindingDBiO64411.

Structurei

Secondary structure

1500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 38Combined sources4
Helixi42 – 53Combined sources12
Beta strandi59 – 62Combined sources4
Beta strandi64 – 69Combined sources6
Beta strandi74 – 77Combined sources4
Beta strandi80 – 85Combined sources6
Beta strandi88 – 96Combined sources9
Helixi100 – 105Combined sources6
Beta strandi112 – 114Combined sources3
Helixi120 – 122Combined sources3
Beta strandi124 – 126Combined sources3
Beta strandi127 – 131Combined sources5
Helixi134 – 156Combined sources23
Helixi168 – 176Combined sources9
Beta strandi178 – 181Combined sources4
Helixi185 – 194Combined sources10
Helixi196 – 199Combined sources4
Turni203 – 205Combined sources3
Beta strandi206 – 208Combined sources3
Turni209 – 211Combined sources3
Helixi215 – 220Combined sources6
Beta strandi222 – 227Combined sources6
Helixi235 – 242Combined sources8
Turni249 – 251Combined sources3
Beta strandi259 – 262Combined sources4
Beta strandi265 – 270Combined sources6
Beta strandi275 – 279Combined sources5
Beta strandi284 – 292Combined sources9
Helixi296 – 300Combined sources5
Beta strandi303 – 308Combined sources6
Helixi312 – 320Combined sources9
Beta strandi321 – 324Combined sources4
Beta strandi326 – 332Combined sources7
Beta strandi345 – 349Combined sources5
Beta strandi352 – 357Combined sources6
Beta strandi359 – 362Combined sources4
Turni364 – 366Combined sources3
Beta strandi367 – 369Combined sources3
Beta strandi372 – 378Combined sources7
Helixi379 – 386Combined sources8
Helixi390 – 404Combined sources15
Beta strandi406 – 408Combined sources3
Beta strandi414 – 417Combined sources4
Turni421 – 423Combined sources3
Turni425 – 427Combined sources3
Beta strandi428 – 433Combined sources6
Helixi440 – 447Combined sources8
Beta strandi453 – 455Combined sources3
Helixi458 – 460Combined sources3
Turni462 – 466Combined sources5
Helixi468 – 488Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO64411.

Family & Domainsi

Sequence similaritiesi

Belongs to the flavin monoamine oxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG0029. Eukaryota.
ENOG410XSNC. LUCA.
HOGENOMiHOG000174927.
KOiK13366.

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.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G034152_P01.

Chemistry databases

BindingDBiO64411.
ChEMBLiCHEMBL6108.

Protein family/group databases

Allergomei955. Zea m PAO.

Proteomic databases

PaxDbiO64411.
PRIDEiO64411.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi541983.
KEGGizma:541983.

Phylogenomic databases

eggNOGiKOG0029. Eukaryota.
ENOG410XSNC. LUCA.
HOGENOMiHOG000174927.
KOiK13366.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-9461.
BRENDAi1.5.3.14. 6752.
SABIO-RKO64411.

Miscellaneous databases

EvolutionaryTraceiO64411.
PROiO64411.

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...

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: November 2, 2016
This is version 115 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

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.