ID   PNAO_PSESP              Reviewed;         497 AA.
AC   H8ZPX1;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2012, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Pseudooxynicotine oxidase;
DE            Short=PNAO;
DE            EC=1.4.3.24;
GN   Name=pao; Synonyms=amo;
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND ACTIVITY REGULATION.
RC   STRAIN=HZN6;
RX   PubMed=22267672; DOI=10.1128/aem.07025-11;
RA   Qiu J., Ma Y., Wen Y., Chen L., Wu L., Liu W.;
RT   "Functional identification of two novel genes from Pseudomonas sp. strain
RT   HZN6 involved in the catabolism of nicotine.";
RL   Appl. Environ. Microbiol. 78:2154-2160(2012).
CC   -!- FUNCTION: Catalyzes the deamination of pseudooxynicotine to 3-
CC       succinoylsemialdehyde-pyridine in the nicotine degradation pathway.
CC       {ECO:0000269|PubMed:22267672}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + pseudooxynicotine = 4-oxo-4-(pyridin-3-yl)butanal +
CC         H2O2 + methylamine; Xref=Rhea:RHEA:33903, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:59338,
CC         ChEBI:CHEBI:66878, ChEBI:CHEBI:66879; EC=1.4.3.24;
CC         Evidence={ECO:0000269|PubMed:22267672};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:22267672};
CC   -!- ACTIVITY REGULATION: Ag(+), Co(2+), Cu(2+) and Hg(2+).
CC       {ECO:0000269|PubMed:22267672}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.247 mM for pseudooxynicotine {ECO:0000269|PubMed:22267672};
CC         Note=kcat is 151 sec(-1) with pseudooxynicotine as substrate.;
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:22267672};
CC   -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC       {ECO:0000269|PubMed:22267672}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; JN391188; AFD54463.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8ZPX1; -.
DR   SMR; H8ZPX1; -.
DR   KEGG; ag:AFD54463; -.
DR   BRENDA; 1.4.3.24; 5085.
DR   UniPathway; UPA00106; -.
DR   GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR   GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IDA:UniProtKB.
DR   GO; GO:0019608; P:nicotine catabolic process; IDA:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR001613; Flavin_amine_oxidase.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase.
FT   CHAIN           1..497
FT                   /note="Pseudooxynicotine oxidase"
FT                   /id="PRO_0000421821"
SQ   SEQUENCE   497 AA;  54101 MW;  710213EE85A8801F CRC64;
     MANDKGDISK DGVSRRKFLG GAVIGAAAAA GVGSQILSLS ATAQGADKER VGPLQSNVDY
     DAVVIGGGFA GVTAARELSR SGLKTLVLEG RSRLGGRTFT SKLDGEKVEL GGTWVHWTQP
     NVWTEVMHYG LEIEETVGLA SPETVIWVTD NQVKRAPAAE AFEIFGAACT EYYKEAHNIY
     PRPFDPFFAK KALQEMDGLS ASEYLNKLSL TREQKDMMDS WLSGNGHNYP ETIAYSEIMR
     WFALSNFNMP TMFDSIARYK IKSGTVSLLE AMVAESDMEV QLSTPVLKVK QDSHRVLITT
     EEGTIAASAV VMAVPLNTMG DVEYSPRLSD AKSEIASQGH AGKGVKGYIR IKQDVGNVMT
     YAPARNDVTP FTSVFTDHVG ENGTLLIAFS ADPKLVDIND SKAVEKALHP LLPGVEVTSS
     YGYDWNLDPF SKGTWCTYRP GQTTRYLTEL QKREGRLFFA GSDMANGWRG FIDGAIESGR
     EVGYQVASYL KGKNSNA