ID   PYRD1_PONAB             Reviewed;         500 AA.
AC   Q5REJ2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1;
DE            EC=1.8.1.-;
GN   Name=PYROXD1;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable FAD-dependent oxidoreductase; involved in the
CC       cellular oxidative stress response (By similarity). Required for normal
CC       sarcomere structure and muscle fiber integrity (By similarity).
CC       {ECO:0000250|UniProtKB:Q6PBT5, ECO:0000250|UniProtKB:Q8WU10}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O52582};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O52582};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WU10}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q3TMV7}. Cytoplasm, myofibril, sarcomere
CC       {ECO:0000250|UniProtKB:Q8WU10}.
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. PYROXD1 subfamily. {ECO:0000305}.
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DR   EMBL; CR857536; CAH89815.1; -; mRNA.
DR   RefSeq; NP_001127199.1; NM_001133727.1.
DR   AlphaFoldDB; Q5REJ2; -.
DR   SMR; Q5REJ2; -.
DR   STRING; 9601.ENSPPYP00000004969; -.
DR   GeneID; 100174254; -.
DR   KEGG; pon:100174254; -.
DR   CTD; 79912; -.
DR   eggNOG; KOG2755; Eukaryota.
DR   InParanoid; Q5REJ2; -.
DR   OrthoDB; 1463391at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 3.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   Pfam; PF07992; Pyr_redox_2; 2.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; FAD; Flavoprotein; NADP; Nucleus; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..500
FT                   /note="Pyridine nucleotide-disulfide oxidoreductase domain-
FT                   containing protein 1"
FT                   /id="PRO_0000327421"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WU10"
SQ   SEQUENCE   500 AA;  55871 MW;  4650445F862200F8 CRC64;
     MEAARPPTTA GKFVVVGGGI AGVTCAEQLA THFPSEDILL VTASPVIKAV TNFKQISKIL
     EEFDVEEQSS TMLEKRFPNI KVIESGVKQL KSEEHCIVTE DGNQHVYKKL CLCAGAKPKL
     ICEGNPYVLG IRDTDSAQEF QKQLIKAKRI MIIGNGGIAL ELVYEIEGCE VIWAIKDKAI
     GNTFFDAGAA EFLTSKLIAE KSEAKIAHKR TRYTTEGRKK EARSKCKSDN VGSALGPDWH
     EGLNLKGTKE FSHKIHLETM CEVKKIYLQD EFRILKKKSF SFPRDHKSVT TDTEMWPVYV
     ELTNEKIYGC DFIVSATGVT PNVEPFLHGN SFELGEDGGL KVDDHMHTSL PDVYAAGDIC
     TTAWQLSPVW QQMRLWTQAR QMGWYAAKCM AAASSGDSID MDFSFELFAH VTKFFNYKVV
     LLGKYNAQGL GSDHELMLRC TKGQEYVKVV MQNGRMMGAV LIGETDLEET FENLILNQMN
     LSSYGEDLLD PNIDIEDYFD