ID   A0A0V0WQ23_9BILA        Unreviewed;       476 AA.
AC   A0A0V0WQ23;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 {ECO:0000256|ARBA:ARBA00018240};
GN   Name=pyroxd1 {ECO:0000313|EMBL:KRX77853.1};
GN   ORFNames=T06_5810 {ECO:0000313|EMBL:KRX77853.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX77853.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX77853.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX77853.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. PYROXD1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008147}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRX77853.1}.
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DR   EMBL; JYDK01000075; KRX77853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0WQ23; -.
DR   Proteomes; UP000054673; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR43429:SF2; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF07992; Pyr_redox_2; 2.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054673}.
FT   DOMAIN          43..170
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          274..359
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   476 AA;  52145 MW;  4FA449068F5CF821 CRC64;
     MQKEYSATFV VVGGGIAGVA CVNELGRVLR SLNFTGAPAS EVFSERPNVN VVQAYITKLD
     RNKKELTASD GTTFKYEKLC IATGGIPKLI SENPNVVCIR DTESVEDFQN RLSGARRIVV
     VGNGGIATEV VGEVTNIEVI WVVKHDTITA TFIDAGAAEF FLPYIHNKSI FTGPNASPTY
     SKDALKARVP PVAGGVSSSG TSEEVDSKFN RGSALGPDWA GDFCMEGSLH GKRIHLEKQC
     SVKAVLTPEQ RKELNLKDEV LPSDFAEIDS WPVYVQLTND KVYGCDFIVS AIGVEPNTYP
     WVTPENDFKV ADDGGLLIDD QMQTNFEDIF AAGDVCTAGW ELDPNWFQMR LWTQAKQMGS
     YAGLCMAMNF AGSKMELDIC FCIFTHVTKF FGFRVILLGK FNGQGLRSDH EALLRVTPGV
     EYVKVLIQDG VVRGAILIGD TGLGDMLENL ILNQTYIEDM KSDLLEPSAD IDDYFD
//