ID   PYRD2_PONAB             Reviewed;         581 AA.
AC   Q5RAP5;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000250|UniProtKB:Q8N2H3};
DE            EC=1.-.-.-;
GN   Name=PYROXD2 {ECO:0000250|UniProtKB:Q8N2H3};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable oxidoreductase that may play a role as regulator of
CC       mitochondrial function. {ECO:0000250|UniProtKB:Q8N2H3}.
CC   -!- SUBUNIT: Interacts with COX5B; this interaction may contribute to
CC       localize PYROXD2 to the inner face of the inner mitochondrial membrane.
CC       {ECO:0000250|UniProtKB:Q8N2H3}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q8N2H3}. Note=The import into mitochondria is
CC       dependent on TOMM40 and TIMM23. {ECO:0000250|UniProtKB:Q8N2H3}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; CR858970; CAH91165.1; -; mRNA.
DR   AlphaFoldDB; Q5RAP5; -.
DR   SMR; Q5RAP5; -.
DR   STRING; 9601.ENSPPYP00000002956; -.
DR   eggNOG; KOG4254; Eukaryota.
DR   InParanoid; Q5RAP5; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome.
FT   CHAIN           1..581
FT                   /note="Pyridine nucleotide-disulfide oxidoreductase domain-
FT                   containing protein 2"
FT                   /id="PRO_0000244073"
FT   BINDING         38..71
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   581 AA;  63045 MW;  4E2E64E5A0295FD5 CRC64;
     MAASGRGLRK AVAASPFPAW RRAHTEAGGG LKPEYDAVVI GAGHNGLVVA AYLQRLGVNT
     AVFERRHVIG GAAVTEEIIP GFKFSRASYL LSLLRPQIYT DLELKKHGLR LHLRNPYSFT
     PMLEEGAGSK VPRSLLLGTD MAENQKQIAQ FSRKDAQVFP RYEEFMHRLA LAIDPLLDAA
     PVDMAAFQRG SLLQRMRSFS TLKPLLKAGR ILGAQLPRYY EVLTAPITKV LDQWFESEPL
     KATLATDAVI GAMTSPHTPG SGYVLLHHVM GGLEGMQGAW GYVQGGMGAL SDAIASSATT
     HGASIFTEKT VAKVQVNSEG CVQGVVLEDG TEVRSKVVLS NTSPQITFLK LTPQEWLPEE
     FLERISQLDT RSPVTKINVA VDRLPSFLAA PNAPRGQPLP HHQCSIHLNC EDTLLLHQAF
     EDAMDGLPSH RPIIELCIPS SLDPPLAPSG CHVVSLFTQY TPYTLAGGKA WDEQERDAYA
     DRVFDCVEVY APGFKDSVVG RDILTPPDLE RIFGLPGGNI FHCAMSLDQL YFARPVPLHS
     GYRCPLQGLY LCGSGAHPGG GVMGAAGRNA AHVAFRDLKS M