ID   A0A1A8Z272_9ACTN        Unreviewed;       530 AA.
AC   A0A1A8Z272;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=GA0070611_0391 {ECO:0000313|EMBL:SBT37975.1};
OS   Micromonospora auratinigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=261654 {ECO:0000313|EMBL:SBT37975.1, ECO:0000313|Proteomes:UP000199385};
RN   [1] {ECO:0000313|Proteomes:UP000199385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44815 {ECO:0000313|Proteomes:UP000199385};
RA   Varghese N.;
RL   Submitted (JUN-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}.
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DR   EMBL; LT594323; SBT37975.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A8Z272; -.
DR   STRING; 261654.GA0070611_0391; -.
DR   PATRIC; fig|261654.4.peg.393; -.
DR   OrthoDB; 833207at2; -.
DR   Proteomes; UP000199385; Chromosome i.
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: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:UP000199385}.
FT   DOMAIN          16..496
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   530 AA;  55530 MW;  DEDAAD82CE50D433 CRC64;
     MIPTADAVVI GAGHNGLVAA NLLADAGWDV LVLEATEAPG GAVRSAQVTA PGYLSDLYSS
     FYPLGYASPV LRGLDLDRHG LRWTHAPDVL AHLLPDGRAA VINRDLATTA ASLEQFAPGD
     GERWEHAYAD WAEVAGPMLD TITTPFPPVR GGLGLLRRLR VGGALRLARR LVVPVRKLGD
     ELFDGEGGPA LLAGCALHTD LSPEEAGSGV YGWLLAMLGQ QVGWPVPVGG AQRITDTLVA
     RLVQRGGRID YNARVDRVLT ARGRAMGVRT VGGATWRARR AVLADVPAPA LFLDLVGAAA
     LPPRLVEDLA HFKWDGSTLK VDWALSAPVP WKNRAVAGAG TVHLGADLNG LTTYAAELAR
     GELPRDPFLL VGQMSVADPS HSPPGTESLW SYTHLPFRPN WRAEDVAAHV TRMEDVLEEA
     APGFRALIVG RHVAGPADLE AGDPSLVGGA LGGGTAAAYQ QLFLRPIPGL GRADTPVDRL
     FLASSSAHPG GGVHGAPGAN AARAALARDR ALTGPLYAGV IDAAHRAVYR
//