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Q865R1 (PAOX_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
EC=1.5.3.13
Alternative name(s):
Polyamine oxidase
Gene names
Name:PAOX
Synonyms:PAO
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Flavoenzyme which catalyzes the oxidation of N(1)-acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine > N1,N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration.

Catalytic activity

N(1)-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2.

N(1)-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2.

N1,N(12)-diacetylspermine + O2 + H2O = N(1)-acetylspermidine + 3-acetamidobutanal + H2O2.

Cofactor

Binds 1 FAD per subunit By similarity.

Pathway

Amine and polyamine metabolism; spermine metabolism.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome By similarity. Cytoplasm By similarity.

Miscellaneous

Oxidizes N(1)-acetylated polyamines on the exo-side of their N(4)-amino groups. Plant PAO oxidizes spermine on the endo-side of the N(4)-nitrogen By similarity.

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 66
PRO_0000236802
Chain7 – 512506Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
PRO_0000099874

Regions

Motif510 – 5123Microbody targeting signal Potential

Experimental info

Sequence conflict71Q → E AA sequence Ref.2
Sequence conflict4821T → P in AAN40707. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q865R1 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: 6164E3A77841F36F

FASTA51256,325
        10         20         30         40         50         60 
MQSGGRQAEA PGRGPRVLVV GGGIAGLGAA QRLCRHPAFS HLRVLEATAR AGGRIRSEHS 

        70         80         90        100        110        120 
FGGVVEVGAH WIHGPSQGNP VFQLAAKYGL LGEKALSEEN QLIETGGHVG LPSVSYASSG 

       130        140        150        160        170        180 
VSVSLELVAE MASLFYSLID QTREFLQAAE TTPPSVGEYL KEKIRQHMAG WTEDEETKKL 

       190        200        210        220        230        240 
KLAILKNLFN VECCVSGTHS MDLVALAPFG EYTVLPGLDC TFPEGYQGLT DCIMASLPKD 

       250        260        270        280        290        300 
VMVFDKPVKT IHWNGSFREA SAPGETFPVL VECEDGDCFP AHHVVVTVPL GFFKKHLDTF 

       310        320        330        340        350        360 
FEPPLPTEKV EAIRKIGFGT NNKIFLEFEE PFWEPDCQHI QVVWEDMSPL EDTAPELQDA 

       370        380        390        400        410        420 
WFKKLIGFWV LPPFQASHVL CGFIAGLESE FMETLSDEDV LRSLTQVLRR VTGNPQLPAP 

       430        440        450        460        470        480 
RSMLRSCWHS APYTRGSYSY VAVGSSGDDM DRLAQPLPSD GKGAQLQVLF AGEATHRTFY 

       490        500        510 
STTHGALLSG WREADRLMTL WDPQAQWPEP RL

« Hide

References

[1]"Comparative mapping of the bovine SPRN locus."
Ferretti L., Uboldi C., Del Vecchio I., Eggen A., Brunner R., Iannuzzi L.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]"Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N(1)-acetylated polyamine oxidase."
Wu T., Yankovskaya V., McIntire W.S.
J. Biol. Chem. 278:20514-20525(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-512, PROTEIN SEQUENCE OF 7-27; 57-76 AND 497-511, CHARACTERIZATION.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ058607 mRNA. Translation: AAY83881.1.
DQ058602 Genomic DNA. Translation: AAY83877.1.
AF226658 mRNA. Translation: AAN40707.1.
IPIIPI00696076.
RefSeqNP_001013620.2. NM_001013602.2.
UniGeneBt.36568.

3D structure databases

ProteinModelPortalQ865R1.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000048799.

Proteomic databases

PRIDEQ865R1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282639.
KEGGbta:282639.

Organism-specific databases

CTD196743.

Phylogenomic databases

eggNOGNOG311398.
HOGENOMHOG000037651.
HOVERGENHBG053499.
KOK00308.

Enzyme and pathway databases

BRENDA1.5.3.11. 908.
UniPathwayUPA00826.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20806320.

Entry information

Entry namePAOX_BOVIN
AccessionPrimary (citable) accession number: Q865R1
Secondary accession number(s): Q4PS79
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 30, 2006
Last modified: April 3, 2013
This is version 61 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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