ID H9B9L9_EIMTE Unreviewed; 382 AA.
AC H9B9L9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF07992};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:AET50679.1};
RN [1] {ECO:0000313|EMBL:AET50679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:AET50679.1};
RX PubMed=22244352; DOI=10.1186/1471-2164-13-21;
RA Amiruddin N., Lee X.W., Blake D.P., Suzuki Y., Tay Y.L., Lim L.S.,
RA Tomley F.M., Watanabe J., Sugimoto C., Wan K.L.;
RT "Characterisation of full-length cDNA sequences provides insights into the
RT Eimeria tenella transcriptome.";
RL BMC Genomics 13:21-21(2012).
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. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; JN987456; AET50679.1; -; mRNA.
DR AlphaFoldDB; H9B9L9; -.
DR VEuPathDB; ToxoDB:ETH2_1319100; -.
DR VEuPathDB; ToxoDB:ETH_00028950; -.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
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; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 36..355
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 382 AA; 40813 MW; C81690368956CA3D CRC64;
MQLHRLAARP LTVPTVHVSA LFRRTHQRSF SSQSEYDVVV IGGGPGGYVA AIKAAQLGLK
TACVEKRGAL GGTCLNVGCI PSKALLNMSH KYKEASSDFS RFGIRVSDVS VDISSMQDYK
DKIVSGLTQG IEGLFKRNKV DYLNGTGRLA GPHAVQVQPI DAGNPQMLMA KNVILATGSE
PAPLAGGALE VDEETIVSST GALALPRVPK HLVVVGGGVI GLELGSVWRN LGAEVTVVEF
CDKIIPALDA EIGRAFQKLL ERQGIKFMFG TKVVGSQKAD GGVTLSLENV KSGDASEVQC
DVVLVAVGRR PYTKDLGLEE LGINLDNRGR VVVNEQMQVP NYPNIMAIGD LIQGVRKTSI
QMFHVYKRTL LTPPSFQAQP DA
//