ID   PNO_MICLT               Reviewed;         507 AA.
AC   Q9AJD6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Pyridoxine 4-oxidase;
DE            EC=1.1.3.12;
GN   Name=pno;
OS   Microbacterium luteolum (Aureobacterium luteolum).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Microbacterium.
OX   NCBI_TaxID=69367;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20 AND 348-364,
RP   CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=YK-1;
RX   PubMed=12092811; DOI=10.1271/bbb.66.1022;
RA   Kaneda Y., Ohnishi K., Yagi T.;
RT   "Purification, molecular cloning, and characterization of pyridoxine 4-
RT   oxidase from Microbacterium.";
RL   Biosci. Biotechnol. Biochem. 66:1022-1031(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pyridoxine = H2O2 + pyridoxal; Xref=Rhea:RHEA:15033,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16709,
CC         ChEBI:CHEBI:17310; EC=1.1.3.12;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=54.5 uM for pyridoxine {ECO:0000269|PubMed:12092811};
CC         KM=206.64 uM for oxygen {ECO:0000269|PubMed:12092811};
CC         KM=9.71 uM for 2,6-dichloroindophenol {ECO:0000269|PubMed:12092811};
CC         KM=50.16 uM for vitamin K3 {ECO:0000269|PubMed:12092811};
CC       pH dependence:
CC         Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:12092811};
CC       Temperature dependence:
CC         Optimum temperature is 40 degrees Celsius.
CC         {ECO:0000269|PubMed:12092811};
CC   -!- PATHWAY: Cofactor degradation; B6 vitamer degradation; pyridoxal from
CC       pyridoxine (oxidase route): step 1/1.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AB049341; BAB39853.1; -; Genomic_DNA.
DR   PIR; JC7855; JC7855.
DR   AlphaFoldDB; Q9AJD6; -.
DR   SMR; Q9AJD6; -.
DR   BRENDA; 1.1.3.12; 7273.
DR   UniPathway; UPA00192; UER00590.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050237; F:pyridoxine 4-oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042820; P:vitamin B6 catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; PTHR11552; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12092811"
FT   CHAIN           2..507
FT                   /note="Pyridoxine 4-oxidase"
FT                   /id="PRO_0000205614"
FT   ACT_SITE        448
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ   SEQUENCE   507 AA;  54196 MW;  64B3A9A094E0AE21 CRC64;
     MAQYDVAIIG AGSAGALIAA RLSEDPARNV LLIEAGGRPS DPDILKPSMW PAIQHRSYDW
     DYKTTPQEGA AGRSFAWARG KGLGGSSLLH AMGYMRGHPA DFAAWAEATG DERWSWEGLL
     PSFMANEDHV SGGDGIHGKD GPMPVWIPDD EVSPLTQAFM TAGNALGLPR IPDHNTGQMI
     GVTPNSLMIR DGRRVTVAEA WLTPEVCARP NLTIMTGTLT RRLKLEKSHV SAIELAGPEG
     LATVTASEII LSAGSLESPA LLMRSGIGRE NVLREAGVTC RVKAPELGLN LMDHLLGAGN
     LYATKKHLPP SRLQHSESMA YMRAGDFSAG GQPEIVVGCG VAPIVSESFT APAPGNAYSF
     LFGVTHPTSR GEIRITGDAP DSPLIIDPRY LQTQNDRNLF RAALGAAREI GHRPELAEWR
     DHEILPKSLA ASQDIDTFIA KAVITHHHPS GTCRMGKDEM SVVDADLRLR GLDNLYVVDG
     SVLPSLTAGP IHAAVQAIAE NFTTGFK