PAOX_BOVIN
ID PAOX_BOVIN Reviewed; 512 AA.
AC Q865R1; Q4PS79;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Peroxisomal N(1)-acetyl-spermine/spermidine oxidase;
DE EC=1.5.3.13 {ECO:0000250|UniProtKB:Q8C0L6};
DE AltName: Full=Polyamine oxidase;
DE Flags: Precursor;
GN Name=PAOX; Synonyms=PAO;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Ferretti L., Uboldi C., Del Vecchio I., Eggen A., Brunner R., Iannuzzi L.;
RT "Comparative mapping of the bovine SPRN locus.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-512, AND PROTEIN SEQUENCE OF 7-27; 57-76
RP AND 497-511.
RC TISSUE=Liver;
RX PubMed=12660232; DOI=10.1074/jbc.m302149200;
RA Wu T., Yankovskaya V., McIntire W.S.;
RT "Cloning, sequencing, and heterologous expression of the murine peroxisomal
RT flavoprotein, N(1)-acetylated polyamine oxidase.";
RL J. Biol. Chem. 278:20514-20525(2003).
CC -!- FUNCTION: Flavoenzyme which catalyzes the oxidation of N(1)-
CC acetylspermine to spermidine and is thus involved in the polyamine
CC back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine.
CC Substrate specificity: N(1)-acetylspermine = N(1)-acetylspermidine >
CC N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine.
CC Plays an important role in the regulation of polyamine intracellular
CC concentration. {ECO:0000250|UniProtKB:Q8C0L6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermine + O2 = 3-acetamidopropanal + H2O2 +
CC spermidine; Xref=Rhea:RHEA:25800, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:58101; EC=1.5.3.13;
CC Evidence={ECO:0000250|UniProtKB:Q8C0L6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1)-acetylspermidine + O2 = 3-acetamidopropanal + H2O2
CC + putrescine; Xref=Rhea:RHEA:25812, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:30322,
CC ChEBI:CHEBI:58324, ChEBI:CHEBI:326268; EC=1.5.3.13;
CC Evidence={ECO:0000250|UniProtKB:Q8C0L6};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(1),N(12)-diacetylspermine + O2 = 3-acetamidopropanal +
CC H2O2 + N(1)-acetylspermidine; Xref=Rhea:RHEA:25868,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:30322, ChEBI:CHEBI:58324, ChEBI:CHEBI:58550; EC=1.5.3.13;
CC Evidence={ECO:0000250|UniProtKB:Q8C0L6};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q8C0L6};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q8C0L6};
CC -!- PATHWAY: Amine and polyamine metabolism; spermine metabolism.
CC {ECO:0000250|UniProtKB:Q8C0L6}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}. Cytoplasm
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Oxidizes N(1)-acetylated polyamines on the exo-side of
CC their N(4)-amino groups. Plant PAO oxidizes spermine on the endo-side
CC of the N(4)-nitrogen (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; DQ058607; AAY83881.1; -; mRNA.
DR EMBL; DQ058602; AAY83877.1; -; Genomic_DNA.
DR EMBL; AF226658; AAN40707.1; -; mRNA.
DR RefSeq; NP_001013620.2; NM_001013602.2.
DR AlphaFoldDB; Q865R1; -.
DR SMR; Q865R1; -.
DR STRING; 9913.ENSBTAP00000048799; -.
DR PaxDb; Q865R1; -.
DR PRIDE; Q865R1; -.
DR GeneID; 282639; -.
DR KEGG; bta:282639; -.
DR CTD; 196743; -.
DR eggNOG; KOG0685; Eukaryota.
DR InParanoid; Q865R1; -.
DR OrthoDB; 508351at2759; -.
DR UniPathway; UPA00826; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0052899; F:N(1),N(12)-diacetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052904; F:N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052903; F:N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IBA:GO_Central.
DR GO; GO:0052902; F:spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0052901; F:spermine:oxygen oxidoreductase (spermidine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0008215; P:spermine metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT PROPEP 1..6
FT /evidence="ECO:0000269|PubMed:12660232"
FT /id="PRO_0000236802"
FT CHAIN 7..512
FT /note="Peroxisomal N(1)-acetyl-spermine/spermidine oxidase"
FT /id="PRO_0000099874"
FT MOTIF 510..512
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 25
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 70..71
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 473
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT BINDING 482..483
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q8C0L6"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6QHF9"
FT CONFLICT 7
FT /note="Q -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="T -> P (in Ref. 2; AAN40707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 56325 MW; 6164E3A77841F36F CRC64;
MQSGGRQAEA PGRGPRVLVV GGGIAGLGAA QRLCRHPAFS HLRVLEATAR AGGRIRSEHS
FGGVVEVGAH WIHGPSQGNP VFQLAAKYGL LGEKALSEEN QLIETGGHVG LPSVSYASSG
VSVSLELVAE MASLFYSLID QTREFLQAAE TTPPSVGEYL KEKIRQHMAG WTEDEETKKL
KLAILKNLFN VECCVSGTHS MDLVALAPFG EYTVLPGLDC TFPEGYQGLT DCIMASLPKD
VMVFDKPVKT IHWNGSFREA SAPGETFPVL VECEDGDCFP AHHVVVTVPL GFFKKHLDTF
FEPPLPTEKV EAIRKIGFGT NNKIFLEFEE PFWEPDCQHI QVVWEDMSPL EDTAPELQDA
WFKKLIGFWV LPPFQASHVL CGFIAGLESE FMETLSDEDV LRSLTQVLRR VTGNPQLPAP
RSMLRSCWHS APYTRGSYSY VAVGSSGDDM DRLAQPLPSD GKGAQLQVLF AGEATHRTFY
STTHGALLSG WREADRLMTL WDPQAQWPEP RL
