ID   U5WC08_9ACTN            Unreviewed;       531 AA.
AC   U5WC08;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=AFR_36175 {ECO:0000313|EMBL:AGZ45491.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ45491.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ45491.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ45491.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ45491.1; -; Genomic_DNA.
DR   RefSeq; WP_023561827.1; NC_022657.1.
DR   AlphaFoldDB; U5WC08; -.
DR   STRING; 1246995.AFR_36175; -.
DR   KEGG; afs:AFR_36175; -.
DR   PATRIC; fig|1246995.3.peg.7320; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_019327_0_1_11; -.
DR   OrthoDB; 9774675at2; -.
DR   Proteomes; UP000017746; Chromosome.
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   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000017746}.
FT   DOMAIN          19..322
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   531 AA;  55486 MW;  8D544203D50E7AA1 CRC64;
     MSALPDRADV VIIGSGHNGL VSAVLLARAG LDVVVLEAAD VIGGATRTEH PFPAVPGLGQ
     STGSYLLGLM PPELLRTLDV DIPVLRRDPH YFLPTPGGPG SPYLLFGTDR EATRAQMERF
     FSPRDVAADE AMQVEIAALR SDLAPAWLQE PGSVEEIADR HIRPQLQSTF IDLVRGSVAD
     YLTRFGFKSE LLMSMYAVTD GLSGLNAGPD DPGTGHNFLV HNMCRLPGSD GTWMIAAGGM
     GTVSRTFADA ARAAGASIFT TSPVSAVTVS GGAATGVVLA DGRSVSAQVV LGACDPYQLM
     SLLPSGALPS SLTTRMEAVR RPGTTLKVNL ALRGLPRFAC LPADAPSPFG STIHLLPGSA
     GLAGLAETDS PMAALRAMWA DVQAGRLPAE PTIEWYLHTT VDPSLQDAAG HHSSALFVQS
     VPYALADSSW DAELPGYVAR LLDIVDRYAP GTSDLVADTM PLTPAGIEKH FGITGGHIHH
     VDNTVSFNER MPYATGLDGL YAGSAGAHPA GSVIGAAGHN AARRILKDLG R
//