ID   K7ZLK3_ONYPH            Unreviewed;       447 AA.
AC   K7ZLK3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Uncharacterized NAD-dependent dehydrogenase {ECO:0000313|EMBL:BAM66623.1};
GN   Name=hcaD {ECO:0000313|EMBL:BAM66623.1};
OS   Onion yellows phytoplasma OY-W.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX   NCBI_TaxID=428984 {ECO:0000313|EMBL:BAM66623.1};
RN   [1] {ECO:0000313|EMBL:BAM66623.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OY-W {ECO:0000313|EMBL:BAM66623.1};
RX   PubMed=22982017; DOI=10.1016/j.gene.2012.09.001;
RA   Miura C., Sugawara K., Neriya Y., Minato N., Keima T., Himeno M.,
RA   Maejima K., Komatsu K., Yamaji Y., Oshima K., Namba S.;
RT   "Functional characterization and gene expression profiling of superoxide
RT   dismutase from plant pathogenic phytoplasma.";
RL   Gene 510:107-112(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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; AB713133; BAM66623.1; -; Genomic_DNA.
DR   AlphaFoldDB; K7ZLK3; -.
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   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          1..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          328..428
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   447 AA;  49491 MW;  458441144394BBF3 CRC64;
     MKVIVVGCTH AGTAAVKTIK KKNPQADVVV YERNDNISFL SCGIALYVGG VIKDSLGLFY
     SNPDELVSMD VCTKLKHEVL KLDFDKKEVL VQSLETGKQF KDNYDKLVIA TGSWPVIPPI
     KGIDCKNVLM SKNFDHAKDI INYSKNVNKI TVVGAGYIGI ELAEAFAVQK KEVVLVDAED
     RIMSKYLDKE FTDVAQKTLT DHGVTLALGQ KIAGFETKDG LVTHVKTDKN TFETEMVIMC
     ISFKPNTQLF AHHLETSFNG ALVVNEYMQT SDPDVYACGD CVNVYYNPTQ EVKYMPLATN
     AIRMGTLVGL NIEKPCLKYL GTQGTSGIKI IDLSISSTGL TENVAKALGK NYGTVTIKDA
     NRPEFMPDYD AVMLKLVFDK DTRKILGGQI VSRVDLTEKM NTLSVCMQNQ MTVEQLAFVD
     FFFQPHFNKP WGLLNLAGLK ALEVKSQ
//