ID Q6YQD3_ONYPE Unreviewed; 447 AA.
AC Q6YQD3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Uncharacterized NAD-dependent dehydrogenase {ECO:0000313|EMBL:BAD04526.1};
GN Name=hcaD {ECO:0000313|EMBL:BAD04526.1};
GN OrderedLocusNames=PAM_441 {ECO:0000313|EMBL:BAD04526.1};
OS Onion yellows phytoplasma (strain OY-M).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX NCBI_TaxID=262768 {ECO:0000313|EMBL:BAD04526.1, ECO:0000313|Proteomes:UP000002523};
RN [1] {ECO:0000313|EMBL:BAD04526.1, ECO:0000313|Proteomes:UP000002523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OY-M {ECO:0000313|Proteomes:UP000002523};
RX PubMed=14661021; DOI=10.1038/ng1277;
RA Oshima K., Kakizawa S., Nishigawa H., Jung H.-Y., Wei W., Suzuki S.,
RA Arashida R., Nakata D., Miyata S., Ugaki M., Namba S.;
RT "Reductive evolution suggested from the complete genome sequence of a
RT plant-pathogenic phytoplasma.";
RL Nat. Genet. 36:27-29(2004).
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}.
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DR EMBL; AP006628; BAD04526.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YQD3; -.
DR STRING; 262768.PAM_441; -.
DR KEGG; poy:PAM_441; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_0_14; -.
DR BioCyc; OYEL262768:G1G26-521-MONOMER; -.
DR Proteomes; UP000002523; Chromosome.
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; 2.
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; 49490 MW; D88308A1E3E89986 CRC64;
MKVIVVGCTH AGTAAVKTIK KNNPQADVVV YERNDNISFL SCGIALYVGG VIKDSLGLFY
SNPDELVSMD VCTKLKHEVL KLNFDKKEVL VQSLETGKQF KDNYDKLVIA TGSWPVIPPI
KGIDCKNVLM SKNFDHAKDI INYSKNVNKI TIVGAGYIGI ELAEAFAVQK KEVVLVDAED
RIMSKYLDKE FTDVAQKTLT DHGVTLALGQ KIAGFETKDG LVTHVKTDKN TFETEMVIMC
ISFKPNTQLF AHHLETSFNG ALVVNEYMQT SDPDVYACGD CVNVYYNPTQ EVKYMPLATN
AIRMGTLVGL NIEKPCVKYL GTQGTSGIKI IDLSISSTGL TENVAKALGK NYGTVTIKDA
NRPEFMPDYD AVMLKLVFDK ETRKILGGQI VSRVDLTEKM NTLSVCMQNQ MTVEQLAFVD
FFFQPHFNKP WGLLNLAGLK ALEVKSQ
//
