ID A4HSF7_LEIIN Unreviewed; 491 AA. AC A4HSF7; A0A2K4YL08; A0A381MC11; DT 01-MAY-2007, integrated into UniProtKB/TrEMBL. DT 01-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Trypanothione reductase {ECO:0000256|ARBA:ARBA00013602}; DE EC=1.8.1.12 {ECO:0000256|ARBA:ARBA00013018}; DE AltName: Full=N(1),N(8)-bis(glutathionyl)spermidine reductase {ECO:0000256|ARBA:ARBA00029937}; GN Name=TRYR {ECO:0000313|EMBL:CAM65344.1}; GN ORFNames=LINJ_05_0350 {ECO:0000313|EMBL:CAM65344.1}; OS Leishmania infantum. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania. OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM65344.1, ECO:0000313|Proteomes:UP000008153}; RN [1] {ECO:0000313|EMBL:CAM65344.1, ECO:0000313|Proteomes:UP000008153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65344.1, RC ECO:0000313|Proteomes:UP000008153}; RX PubMed=17572675; DOI=10.1038/ng2053; RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A., RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A., RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T., RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R., RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S., RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P., RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K., RA Mottram J.C., Smith D.F., Berriman M.; RT "Comparative genomic analysis of three Leishmania species that cause RT diverse human disease."; RL Nat. Genet. 39:839-847(2007). RN [2] {ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H} RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH FAD AND NADP, AND RP DISULFIDE BONDS. RX PubMed=19317451; DOI=10.1021/JM900185Q; RA Baiocco P., Colotti G., Franceschini S., Ilari A.; RT "Molecular basis of antimony treatment in leishmaniasis."; RL J. Med. Chem. 52:2603-2612(2009). RN [3] {ECO:0007829|PDB:2X50} RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-490 IN COMPLEX WITH FAD AND RP NADPH. RX PubMed=24900299; DOI=10.1021/ML1002629; RA Baiocco P., Ilari A., Ceci P., Orsini S., Gramiccia M., Di Muccio T., RA Colotti G.; RT "Inhibitory Effect of Silver Nanoparticles on Trypanothione Reductase RT Activity and Leishmania infantum Proliferation."; RL ACS Med. Chem. Lett. 2:230-233(2011). RN [4] {ECO:0000313|EMBL:CAM65344.1, ECO:0000313|Proteomes:UP000008153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM65344.1, RC ECO:0000313|Proteomes:UP000008153}; RX PubMed=22038252; DOI=10.1101/gr.122945.111; RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A., RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D., RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F., RA Hertz-Fowler C., Mottram J.C.; RT "Chromosome and gene copy number variation allow major structural change RT between species and strains of Leishmania."; RL Genome Res. 21:2129-2142(2011). RN [5] {ECO:0007829|PDB:2YAU} RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN COMPLEX WITH FAD AND NADP, AND RP DISULFIDE BONDS. RX PubMed=21833767; DOI=10.1007/S00726-011-0997-9; RA Ilari A., Baiocco P., Messori L., Fiorillo A., Boffi A., Gramiccia M., RA Di Muccio T., Colotti G.; RT "A gold-containing drug against parasitic polyamine metabolism: the X-ray RT structure of trypanothione reductase from Leishmania infantum in complex RT with auranofin reveals a dual mechanism of enzyme inhibition."; RL Amino Acids 42:803-811(2012). RN [6] {ECO:0007829|PDB:4ADW, ECO:0007829|PDB:4APN} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH FAD AND NADPH. RX PubMed=23733388; DOI=10.1002/CMDC.201300176; RA Baiocco P., Poce G., Alfonso S., Cocozza M., Porretta G.C., Colotti G., RA Biava M., Moraca F., Botta M., Yardley V., Fiorillo A., Lantella A., RA Malatesta F., Ilari A.; RT "Inhibition of Leishmania infantum trypanothione reductase by azole-based RT compounds: a comparative analysis with its physiological substrate by X-ray RT crystallography."; RL ChemMedChem 8:1175-1183(2013). RN [7] {ECO:0007829|PDB:5EBK} RP X-RAY CRYSTALLOGRAPHY (3.51 ANGSTROMS) IN COMPLEX WITH FAD, AND DISULFIDE RP BONDS. RX PubMed=28098499; DOI=10.1080/14756366.2016.1250755; RA Saccoliti F., Angiulli G., Pupo G., Pescatori L., Madia V.N., Messore A., RA Colotti G., Fiorillo A., Scipione L., Gramiccia M., Di Muccio T., RA Di Santo R., Costi R., Ilari A.; RT "Inhibition of Leishmania infantum trypanothione reductase by diaryl RT sulfide derivatives."; RL J. Enzym. Inhib. Med. Chem. 32:304-310(2017). RN [8] {ECO:0007829|PDB:6ER5} RP X-RAY CRYSTALLOGRAPHY (3.37 ANGSTROMS) OF 1-488, AND DISULFIDE BONDS. RX PubMed=30475811; DOI=10.1371/journal.pntd.0006969; RA Turcano L., Torrente E., Missineo A., Andreini M., Gramiccia M., RA Di Muccio T., Genovese I., Fiorillo A., Harper S., Bresciani A., RA Colotti G., Ilari A.; RT "Identification and binding mode of a novel Leishmania Trypanothione RT reductase inhibitor from high throughput screening."; RL PLoS Negl. Trop. Dis. 12:e0006969-e0006969(2018). RN [9] {ECO:0007829|PDB:6I7N} RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=30983322; DOI=10.1021/acsinfecdis.8b00355; RA Revuelto A., Ruiz-Santaquiteria M., de Lucio H., Gamo A., Carriles A.A., RA Gutierrez K.J., Sanchez-Murcia P.A., Hermoso J.A., Gago F., Camarasa M.J., RA Jimenez-Ruiz A., Velazquez S.; RT "Pyrrolopyrimidine vs Imidazole-Phenyl-Thiazole Scaffolds in Nonpeptidic RT Dimerization Inhibitors of Leishmania infantum Trypanothione Reductase."; RL ACS Infect. Dis. 5:873-891(2019). RN [10] {ECO:0007829|PDB:6T97} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-488, AND DISULFIDE BONDS. RA Revuelto A., de Lucio H., Carriles A., Garcia Soriano J.C., RA Sanchez-Murcia P.A., Hermoso J.A., Gago F., Camarasa M.J., Jimenez-Ruiz A., RA Velazquez S.; RT "Scaffold hopping identifies new triazole-and triazolium-based inhibitors RT of Leishmania infantum Trypanothione Reductase with potent and selective RT antileishmanial activity."; RL Submitted (OCT-2019) to the PDB data bank. RN [11] {ECO:0007829|PDB:6T95, ECO:0007829|PDB:6T98} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-488, AND DISULFIDE BONDS. RX PubMed=36332553; DOI=10.1016/j.ejmech.2022.114878; RA de Lucio H., Revuelto A., Carriles A.A., de Castro S., Garcia-Gonzalez S., RA Garcia-Soriano J.C., Alcon-Calderon M., Sanchez-Murcia P.A., Hermoso J.A., RA Gago F., Camarasa M.J., Jimenez-Ruiz A., Velazquez S.; RT "Identification of 1,2,3-triazolium salt-based inhibitors of Leishmania RT infantum trypanothione disulfide reductase with enhanced antileishmanial RT potency in cellulo and increased selectivity."; RL Eur. J. Med. Chem. 244:114878-114878(2022). CC -!- FUNCTION: Trypanothione is the parasite analog of glutathione; this CC enzyme is the equivalent of glutathione reductase. CC {ECO:0000256|ARBA:ARBA00003667}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NADP(+) + trypanothione = H(+) + NADPH + trypanothione CC disulfide; Xref=Rhea:RHEA:16757, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58290, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:58661; EC=1.8.1.12; CC Evidence={ECO:0000256|ARBA:ARBA00001054}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3}; CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532, CC ECO:0000256|RuleBase:RU003691}. 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; FR796437; CAM65344.1; -; Genomic_DNA. DR RefSeq; XP_001462998.1; XM_001462961.1. DR PDB; 2JK6; X-ray; 2.95 A; A/B=1-491. DR PDB; 2W0H; X-ray; 3.00 A; A/B=1-491. DR PDB; 2X50; X-ray; 3.30 A; A/B=1-490. DR PDB; 2YAU; X-ray; 3.50 A; A/B=1-491. DR PDB; 4ADW; X-ray; 3.61 A; A/B=1-491. DR PDB; 4APN; X-ray; 3.20 A; A/B=1-491. DR PDB; 5EBK; X-ray; 3.51 A; A/B=1-491. DR PDB; 6ER5; X-ray; 3.37 A; A=1-488. DR PDB; 6I7N; X-ray; 3.30 A; A/B=1-491. DR PDB; 6T95; X-ray; 2.50 A; A=1-488. DR PDB; 6T97; X-ray; 2.80 A; A=1-488. DR PDB; 6T98; X-ray; 3.00 A; A=1-488. DR PDBsum; 2JK6; -. DR PDBsum; 2W0H; -. DR PDBsum; 2X50; -. DR PDBsum; 2YAU; -. DR PDBsum; 4ADW; -. DR PDBsum; 4APN; -. DR PDBsum; 5EBK; -. DR PDBsum; 6ER5; -. DR PDBsum; 6I7N; -. DR AlphaFoldDB; A4HSF7; -. DR SMR; A4HSF7; -. DR STRING; 5671.A4HSF7; -. DR BindingDB; A4HSF7; -. DR ChEMBL; CHEMBL1944501; -. DR GeneID; 5066544; -. DR KEGG; lif:LINJ_05_0350; -. DR VEuPathDB; TriTrypDB:LINF_050008500; -. DR eggNOG; KOG0405; Eukaryota. DR InParanoid; A4HSF7; -. DR OMA; VHIIHHN; -. DR OrthoDB; 5473641at2759; -. DR BRENDA; 1.8.1.12; 2949. DR EvolutionaryTrace; A4HSF7; -. DR Proteomes; UP000008153; Chromosome 5. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0015042; F:trypanothione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC. DR GO; GO:0045454; P:cell redox homeostasis; 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; IPR046952; GSHR/TRXR-like. DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR012999; Pyr_OxRdtase_I_AS. DR InterPro; IPR001864; Trypnth_redctse. DR NCBIfam; TIGR01423; trypano_reduc; 1. DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1. DR PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR PRINTS; PR00470; TRYPANRDTASE. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1. DR SUPFAM; SSF51971; Nucleotide-binding domain; 1. DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|RuleBase:RU003691}; NAD {ECO:0000256|PIRSR:PIRSR000350-3}; KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0007829|PDB:2JK6}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|RuleBase:RU003691}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|RuleBase:RU003691}; KW Reference proteome {ECO:0000313|Proteomes:UP000008153}. FT DOMAIN 5..342 FT /note="FAD/NAD(P)-binding" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 363..468 FT /note="Pyridine nucleotide-disulphide oxidoreductase FT dimerisation" FT /evidence="ECO:0000259|Pfam:PF02852" FT ACT_SITE 461 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2" FT BINDING 14 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 14 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 15 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 15 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 16 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:5EBK, ECO:0007829|PDB:6ER5" FT BINDING 35 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 35 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 47 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2W0H, ECO:0007829|PDB:4APN" FT BINDING 51 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 51 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 52 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 60 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 60 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 60 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 61 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 127 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 127 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 127 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 160..162 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 195..202 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 196 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 196 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4ADW" FT BINDING 196 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:4ADW" FT BINDING 198 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:6T97" FT BINDING 198 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4APN" FT BINDING 199 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4ADW" FT BINDING 199 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 199 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H, ECO:0007829|PDB:4ADW" FT BINDING 202 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H" FT BINDING 221 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H, ECO:0007829|PDB:4ADW" FT BINDING 221 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 221 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4ADW" FT BINDING 222 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H, ECO:0007829|PDB:4ADW" FT BINDING 222 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 222 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4ADW" FT BINDING 228 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4ADW" FT BINDING 228 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H, ECO:0007829|PDB:4ADW" FT BINDING 254 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H, ECO:0007829|PDB:4ADW" FT BINDING 254 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4ADW" FT BINDING 254 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 286 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 286 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4APN" FT BINDING 327 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 327 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3" FT BINDING 327 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 333 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 333 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4APN" FT BINDING 333 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H" FT BINDING 335 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT BINDING 335 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 365 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2X50, ECO:0007829|PDB:4ADW" FT BINDING 365 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2YAU" FT BINDING 365 FT /ligand="NADPH" FT /ligand_id="ChEBI:CHEBI:57783" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2W0H, ECO:0007829|PDB:4ADW" FT BINDING 461 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:2W0H" FT BINDING 461 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:6I7N" FT DISULFID 52..57 FT /evidence="ECO:0007829|PDB:2JK6, ECO:0007829|PDB:5EBK" FT DISULFID 52..57 FT /note="Redox-active" FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4" FT DISULFID 89..213 FT /evidence="ECO:0007829|PDB:2YAU, ECO:0007829|PDB:5EBK" FT DISULFID 444 FT /note="Interchain" FT /evidence="ECO:0007829|PDB:6I7N" SQ SEQUENCE 491 AA; 53026 MW; 1E41FDC657DDCF67 CRC64; MSRAYDLVVL GAGSGGLEAG WNAAVTHKKK VAVVDVQATH GPPLFAALGG TCVNVGCVPK KLMVTGAQYM DLIRESGGFG WEMDRESLCP NWKTLIAAKN KVVNSINESY KSMFADTEGL SFHMGFGALQ DAHTVVVRKS EDPHSDVLET LDTEYILIAT GSWPTRLGVP GDEFCITSNE AFYLEDAPKR MLCVGGGYIA VEFAGIFNGY KPCGGYVDLC YRGDLILRGF DTEVRKSLTK QLGANGIRVR TNLNPTKITK NEDGSNHVHF NDGTEEDYDQ VMLAIGRVPR SQALQLDKAG VRTGKNGAVQ VDAYSKTSVD NIYAIGDVTN RVMLTPVAIN EGAAFVETVF GGKPRATDHT KVACAVFSIP PIGTCGMTEE EAAKNYETVA VYASSFTPLM HNISGSKHKE FMIRIITNES NGEVLGVHML GDSAPEIIQS VGICMKMGAK ISDFHSTIGV HPTSAEELCS MRTPAYFYES GKRVEKLSSN L //