ID   A0A1H5T1G3_9ACTN        Unreviewed;       533 AA.
AC   A0A1H5T1G3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=SAMN05216223_101355 {ECO:0000313|EMBL:SEF56663.1};
OS   Actinacidiphila yanglinensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310779 {ECO:0000313|EMBL:SEF56663.1, ECO:0000313|Proteomes:UP000236754};
RN   [1] {ECO:0000313|EMBL:SEF56663.1, ECO:0000313|Proteomes:UP000236754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2023 {ECO:0000313|EMBL:SEF56663.1,
RC   ECO:0000313|Proteomes:UP000236754};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FNVU01000001; SEF56663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5T1G3; -.
DR   Proteomes; UP000236754; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10668:SF103; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000236754}.
FT   DOMAIN          7..286
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   533 AA;  56640 MW;  DF03280D38EC9A10 CRC64;
     MGGGHNGLVA ATYLAKAGRS VLLLERLPAT GGAAVSTRAF HGVDARLSRY SYLVSLLPRK
     IVDDLDLRFA VRRRRISSYT PHGDAGLLVD AEDSARTREQ FVRLTGSERD FDAWQRFYAM
     TGEVARRVFP TLTEPLPTRA ELERRVGDAT AWEALFERPL GETVEATFSD DVVRGVVLTD
     ALIGTFTHAH DPSLRQNRCF VYHVIGGGTG DWDVPIGGMG AFTDALAAAA RAAGVRIVTG
     AEVTAIATDG KVAEVTYEDV EGGGTRTVGA RDVLVNASPH ALAGLLGAER PPRPEGAQLK
     VNMLLRRLPR LRDTSVDPRE AFAGTFHIAE GYRQLQTAYE QAAAGRVPDA PPSEIYCHSL
     TDPSILSPEL AAAGTHTLTL FGLHAPARLF ATDPQRVKEE LLAATLAQLD AVLAEPLADC
     LATDADGRPC LEAKSPLDLE REVGLPGGHI FHRDLSWPYA DEDADADRGG NADAAGGNGE
     RLAHVDVTQA TGRWGVGTGY ANVFLCGAGA VRGGGVSGVP GHNAARAVLE RAR
//