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Database: UniProt
Entry: A0A1I4WYE2_9GAMM
LinkDB: A0A1I4WYE2_9GAMM
Original site: A0A1I4WYE2_9GAMM 
ID   A0A1I4WYE2_9GAMM        Unreviewed;       533 AA.
AC   A0A1I4WYE2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   ORFNames=SAMN05216289_106148 {ECO:0000313|EMBL:SFN18146.1};
OS   Dokdonella immobilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dokdonella.
OX   NCBI_TaxID=578942 {ECO:0000313|EMBL:SFN18146.1, ECO:0000313|Proteomes:UP000198575};
RN   [1] {ECO:0000313|EMBL:SFN18146.1, ECO:0000313|Proteomes:UP000198575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.7659 {ECO:0000313|EMBL:SFN18146.1,
RC   ECO:0000313|Proteomes:UP000198575};
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}.
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DR   EMBL; FOVF01000006; SFN18146.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4WYE2; -.
DR   STRING; 578942.SAMN05216289_106148; -.
DR   OrthoDB; 9774675at2; -.
DR   Proteomes; UP000198575; 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:UP000198575}.
FT   DOMAIN          19..327
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   533 AA;  57112 MW;  48F0A38A37A56EE6 CRC64;
     MNRESGRRDA LIIGGGHNGL VCATYLARAG LQVTVLERRD VVGGAAVTEE FHPGFRNSVA
     SYTVSLLQPK VIRDLDLHAH GLRIVERRLG NFLPLPDGRS LRVGAGLTQA EVAKFSKRDA
     ERLPEYERRL EAIADVLRAL VLEAPPNVSD GGWWKALPEL LRAGRLGRRL HSLDPGLRQE
     LLDLLSISAA EYLDRWFESE PIKAVFGFDG IVGNYASPYT PGSAYVLLHH VFGEVNGVKG
     AWGHAIGGMG AITQAMAKAA EAAGVEIRTG CGVREVIVEN GRAVGVVSET SDVLHARAIV
     ANVNPKLLYE RLMARDVVPQ PTRERMANWR CGSGTFRMNV ALAELPSFTA LPGPGDHLTA
     GIIMAPSLAY MDRAYTDALA TGWSREPIVE MLIPSTLDDS LAPPGRHVAS LFCQQVAPQL
     SDGRSWDDHR DAVADLMIAT VDAYAPGFKA SVLGRQALTP FDLERTFGLV GGDIFHGALS
     LNQLFSARPM LGQANYRGAL PGLYLCGAGT HPGGGVTGAP GHNAARAIVA DLK
//
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