ID   A0A2R8BZ72_9RHOB        Unreviewed;       521 AA.
AC   A0A2R8BZ72;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   Name=crtN {ECO:0000313|EMBL:SPJ25439.1};
GN   ORFNames=PAA8504_03290 {ECO:0000313|EMBL:SPJ25439.1};
OS   Palleronia abyssalis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Palleronia.
OX   NCBI_TaxID=1501240 {ECO:0000313|EMBL:SPJ25439.1, ECO:0000313|Proteomes:UP000244912};
RN   [1] {ECO:0000313|EMBL:SPJ25439.1, ECO:0000313|Proteomes:UP000244912}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8504 {ECO:0000313|EMBL:SPJ25439.1,
RC   ECO:0000313|Proteomes:UP000244912};
RA   Keele B.F.;
RL   Submitted (MAR-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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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; ONZF01000009; SPJ25439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8BZ72; -.
DR   OrthoDB; 9774675at2; -.
DR   Proteomes; UP000244912; Unassembled WGS sequence.
DR   GO; GO:0140868; F:4,4'-diapophytoene desaturase (4,4'-diapolycopene-forming); IEA:UniProtKB-EC.
DR   GO; GO:0102223; F:4,4'-diapophytoene desaturase (4,4'-diaponeurosporene-forming); IEA:UniProtKB-EC.
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   InterPro; IPR001613; Flavin_amine_oxidase.
DR   PANTHER; PTHR10668:SF105; DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10668; PHYTOENE DEHYDROGENASE; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:SPJ25439.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244912}.
FT   DOMAIN          14..335
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   521 AA;  54509 MW;  B4CE952E6C2400C0 CRC64;
     MSRDVVVIGS GINGLVAAAL LAKKGRKVLL LERESQLGGC MRTAEITAPG FLHDVMATTF
     VLFLTGPAYA VLGDDLARHG VEFAHTDHPT AVLRPGGSSV VLTTDRAKNV AALEALAAGD
     GVAFAQAADG VGANADLIFG LLGQGLWSRQ TATLLAREAW RRGARGLAAF LGEGLAPARG
     WLETAFTSET SRALFAPWVL HCGLGPESAY SAQMGKVIAF ALEAAGAPVV KGGAARLVEG
     MRAIIEENGG TIRTDAPVER IETSGGAATG VRLAGGERIA ADHVIASVAP GQLYDQLLDD
     PPAEPAKAAK TFRHGMGNFQ MHYALDAPPR WKTPGMEKVA LVHVTPGLDG VSKAVNEAAR
     GMLPETPTIC VGQSSALDPS RVPEGKATLW LQMPEAPVQI KGDAAGMIDV PADGRWTDAL
     REEYADRIEA ILARHIDGFR DSVIARSAHS PADLQAMNVN LVGGDPYGGS CALDQFFLWR
     PFKGAVNHRT EIRNLWHIGA STHPGPGLGG GSGVLVANRI K
//