ID   A0A077ZP13_STYLE        Unreviewed;       574 AA.
AC   A0A077ZP13;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 {ECO:0000256|ARBA:ARBA00040298};
GN   Name=Contig13954.g14889 {ECO:0000313|EMBL:CDW71204.1};
GN   ORFNames=STYLEM_144 {ECO:0000313|EMBL:CDW71204.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW71204.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW71204.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW71204.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) 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   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00006046}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CCKQ01000133; CDW71204.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077ZP13; -.
DR   EnsemblProtists; CDW71204; CDW71204; STYLEM_144.
DR   InParanoid; A0A077ZP13; -.
DR   OMA; GLYHCGS; -.
DR   OrthoDB; 179056at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000039865}.
FT   DOMAIN          205..355
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   574 AA;  64445 MW;  BDDCDAFC9F3E559B CRC64;
     MLKTISNTYK QHQSTLAKQL LSRQFSTYQE KYDAIIIGAG HNGLICSNYL AKENMKVLVL
     ENRHIVGGAA VSEEIFPGYV FSRASYLLSL LRNNIIKEIF PPNWRDELVL YRRYYPSFTP
     TKQSGTDKYL LLGHDDELKE IAKFSTKDAK NYQDYVNKLD EIVDIINPII DNAPPEGLID
     TIKLGLKIKK PKLQSNTEIF QMMTAPVSTV LDQYFESDIL KATLASDGVI GAMGSPYSQG
     SSYILLHHVM GEIDGKNRWY YVKGGMGSIT QYLAKLAEEK GVTIRTNSQV SQIFTSGDKV
     SGVRLHDGTV INAPIVISNA THHVTFNQLI KEQSAVPDNY QKILKNVNYE GSACKINLVL
     NDLPKFKCIE HINDKAKHAK NMREKMGIYN NYLQGTTHIN SEHMRDIHDA YLDALNGEIC
     RRPMVEMVIP QILDPSLNKN NDENVVCSLF VQYAPTKLKN GKEWDEESRN QFVKNTFDVI
     EEYAPGFSKS VVHKDVLLPP DLERIFGLTG GNIFHGALSM NNVYFSRPGP GYANSNTPFR
     NLFMCGSGQH AGGGVMGVAG RLCAKKVLQQ RKKL
//