ID   A0A3A1P0S9_9SPHN        Unreviewed;       525 AA.
AC   A0A3A1P0S9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=D2V17_15245 {ECO:0000313|EMBL:RIV82405.1};
OS   Aurantiacibacter xanthus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=1784712 {ECO:0000313|EMBL:RIV82405.1, ECO:0000313|Proteomes:UP000265366};
RN   [1] {ECO:0000313|EMBL:RIV82405.1, ECO:0000313|Proteomes:UP000265366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AB 2015396 {ECO:0000313|EMBL:RIV82405.1,
RC   ECO:0000313|Proteomes:UP000265366};
RA   Fang C., Wu Y.-H., Sun C., Wang H., Cheng H., Meng F.-X., Wang C.-S.,
RA   Xu X.-W.;
RT   "Erythrobacter zhengii sp.nov., a bacterium isolated from deep-sea
RT   sediment.";
RL   Submitted (AUG-2018) 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:RIV82405.1}.
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DR   EMBL; QXFM01000118; RIV82405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A1P0S9; -.
DR   OrthoDB; 9774675at2; -.
DR   Proteomes; UP000265366; 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:SF105; DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 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:UP000265366}.
FT   DOMAIN          15..316
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   525 AA;  56752 MW;  9A02F5BA059A8FA2 CRC64;
     MSDADIIVIG AGHNGLVAAA YLAVAGKRVL VLERNAWLGG GVVSRELTEP GFLHDQHSMS
     HIFIQGNPLL LNDDLGLKRK YGLKYVFPEV PMMSVWEDGA TLPLHRDPAK SAEAIARFSR
     KDADTFLAMS QQAAQWLPMI QAGLYAPPMP VGAQAAMMDQ SAEGQEIMRT MAVSTFDLME
     ELFEHDKVKA HFGRVAGENL VSPDEKATGI GAYVFLGFLE KFGFGVPVGG SGSLTKALVA
     CIEDHGGAVR SGCEVREVFT DGSRASGVVL DSGERLTCAD GVIGALHPHI LPDVVPSLPA
     EVARKAKRTH ITDAACFTVH AALDAPMQFK ARNADGSPLS AVMYELMPAS YEDMRRAFDE
     LRYGNFSETP LVGVGQLPQH DPSRCPEGRS IFHAWDYVPY SRKDGRDWDE AKGEFAETMI
     ARMGNYIENV PEAVLSYHCD SPVDMERTSP SFLRGDLHGI ATTTYQSGRH RPTPDLGGYR
     VPGVERLYLV GPFQHPGGGV FGAGRATAMV MAEDLGIDFD GISVG
//