ID A0A1U7Q5V0_MESAU Unreviewed; 581 AA.
AC A0A1U7Q5V0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN Name=Pyroxd2 {ECO:0000313|RefSeq:XP_005063631.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005063631.1};
RN [1] {ECO:0000313|RefSeq:XP_005063631.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006046}.
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DR RefSeq; XP_005063631.1; XM_005063574.3.
DR AlphaFoldDB; A0A1U7Q5V0; -.
DR STRING; 10036.ENSMAUP00000019555; -.
DR GeneID; 101842110; -.
DR KEGG; maua:101842110; -.
DR CTD; 84795; -.
DR eggNOG; KOG4254; Eukaryota.
DR OrthoDB; 179056at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
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 Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706}.
FT DOMAIN 261..389
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 581 AA; 63462 MW; 7F0758E1AC0A717E CRC64;
MAASLRGLSR ALHSSPCPAW KRTQSGAEGH LKAEYDAVVI GAGHNGLVAA AYLQRLGVNT
VVLERRHVIG GAAVTEEIIP GFRFSRASYL LSLLRPQIYT DLELKKHGLR LHFRNPYSFT
PMLEEGTLSK SPRSLLLGTD MAENQRQISQ FSQKDAQAFP RYEEFMRRLV LAIDPLLDAA
PVNTAAFQRG SLLQRLRALS TLRPLLKAGR TLGAQLPQYY QVLTGPISKV LDHWFESEPL
KATLATDAVI GAMTSPHTPG SGYVLLHHVM GNLEGMQGAW SYVQGGMGAL SDAIASSATT
HGASIFTEKP VTKVQVNSEG HVQGVVLQDG QEVRSRVVLS CASPQVTFLE LTPQEWLPES
FVKRISQLDT QSPVTKINVA VDRLPNFRAA PNVPGDQPQP HHQCSIHLNC EDTLVLHQAF
EDAKGGLPSQ RPMIELCIPS SLDPTLAPPG CHVVSLFTQY TPYTLAGGKI WDEQEKNNYA
DKVFDCVEDY APGFKSSVLA RDILTPRDLE RIFSLPGGNI FHGAMSLDQL YFPRPVPQHS
GYRCPIRGLY LCGSGAHPGG GIMGAAGRNA AHEVFRDLKS M
//
