ID   A0A0S9R7G8_9ACTN        Unreviewed;       474 AA.
AC   A0A0S9R7G8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=ASF37_05335 {ECO:0000313|EMBL:KQP78038.1};
OS   Aeromicrobium sp. Leaf289.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736324 {ECO:0000313|EMBL:KQP78038.1, ECO:0000313|Proteomes:UP000051640};
RN   [1] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf289 {ECO:0000313|Proteomes:UP000051640};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable oxidoreductase that may play a role as regulator of
CC       mitochondrial function. {ECO:0000256|ARBA:ARBA00037217}.
CC   -!- SUBUNIT: Interacts with COX5B; this interaction may contribute to
CC       localize PYROXD2 to the inner face of the inner mitochondrial membrane.
CC       {ECO:0000256|ARBA:ARBA00038825}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQP78038.1}.
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DR   EMBL; LMNK01000002; KQP78038.1; -; Genomic_DNA.
DR   RefSeq; WP_056557096.1; NZ_LMNK01000002.1.
DR   AlphaFoldDB; A0A0S9R7G8; -.
DR   OrthoDB; 833207at2; -.
DR   Proteomes; UP000051640; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.90.660.50; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10668:SF105; DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051640}.
FT   DOMAIN          13..246
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   474 AA;  49853 MW;  CADAE8E822BC6094 CRC64;
     MTSAVVVGSG PNGLAGAVRL AQEGLDVTVL EAADRVGGGT RTSELTVPGV LHDECSAFHP
     MGVASPYLAS LELERNGLRW LWPEVDLAHP LDDGRAGVVS RDMERTAASL GADARSWKKL
     FGPITRDFDD LLADVLRPVV HVPSHPLTLA RFGLQAALPA NVLVRRFDDE PARSLFMGVA
     AHVFGRLDTP LSASVGLMLG AAGHRYGWPV AEGGSGSIAA ALVARLEELG GTVRTGVEVT
     SMGQLAEEIG TRPDVILLDT SPRGALGIVG DAIPPLVARQ LRGYRYGPAA FKIDVAIDGE
     IPWTNDEVRR AGTVHVGGSA AEIVDAEGRT ARGVMPDRPF VLLGQQHLAD PSRSRDGINP
     IWAYAHVPHA WPGDATDLIL GQVERFAPGF RDRVVQVVSK GTAQLEAGNA NYVGGDIGTG
     ANTWRQIPLR PRPTLDPYSL GVDGVYLCSA ATPPGGGVHG MGGFNAAEAA LRRL
//