ID   NCPR1_ARATH             Reviewed;         692 AA.
AC   Q9SB48; Q39035;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=NADPH--cytochrome P450 reductase 1 {ECO:0000255|HAMAP-Rule:MF_03212};
DE            Short=AtCPR1 {ECO:0000303|PubMed:31138208};
DE            Short=CPR 1 {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000303|PubMed:31138208, ECO:0000303|PubMed:9235908};
DE            Short=P450R 1 {ECO:0000255|HAMAP-Rule:MF_03212};
DE            EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
DE   AltName: Full=Cytochrome P450 73 A5 {ECO:0000303|PubMed:9235908};
GN   Name=ATR1 {ECO:0000303|PubMed:9235908, ECO:0000303|PubMed:9990323};
GN   Synonyms=AR1 {ECO:0000303|PubMed:9449848}, CYP73A5
GN   {ECO:0000303|PubMed:9235908};
GN   OrderedLocusNames=At4g24520 {ECO:0000312|Araport:AT4G24520};
GN   ORFNames=F22K18.280 {ECO:0000312|EMBL:CAA23011.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9235908; DOI=10.1074/jbc.272.31.19176;
RA   Urban P., Mignotte C., Kazmaier M., Delorme F., Pompon D.;
RT   "Cloning, yeast expression, and characterization of the coupling of two
RT   distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases
RT   with P450 CYP73A5.";
RL   J. Biol. Chem. 272:19176-19186(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX   PubMed=9990323; DOI=10.1046/j.1432-1327.1998.2581040.x;
RA   Louerat-Oriou B., Perret A., Pompon D.;
RT   "Differential redox and electron-transfer properties of purified yeast,
RT   plant and human NADPH-cytochrome P-450 reductases highly modulate
RT   cytochrome P-450 activities.";
RL   Eur. J. Biochem. 258:1040-1049(1998).
RN   [6]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX   PubMed=9449848; DOI=10.1104/pp.116.1.357;
RA   Mizutani M., Ohta D.;
RT   "Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana.
RT   Gene structure, heterologous expression in insect cells, and differential
RT   regulation.";
RL   Plant Physiol. 116:357-367(1998).
RN   [7]
RP   FUNCTION.
RX   PubMed=10208644;
RA   Louerat-Oriou B., Flinois J.P., Beaune P.H., Pompon D.;
RT   "High yield purification and characterization of engineered human P450 1A2
RT   and generation of immuno-inhibitor antibodies.";
RL   Pharmacogenetics 9:61-70(1999).
RN   [8]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9880378; DOI=10.1104/pp.119.1.353;
RA   Fukuchi-Mizutani M., Mizutani M., Tanaka Y., Kusumi T., Ohta D.;
RT   "Microsomal electron transfer in higher plants: cloning and heterologous
RT   expression of NADH-cytochrome b5 reductase from Arabidopsis.";
RL   Plant Physiol. 119:353-361(1999).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
RP   BIOTECHNOLOGY, AND REVIEW.
RX   PubMed=31138208; DOI=10.1186/s12934-019-1138-5;
RA   Wang C., Su X., Sun M., Zhang M., Wu J., Xing J., Wang Y., Xue J., Liu X.,
RA   Sun W., Chen S.;
RT   "Efficient production of glycyrrhetinic acid in metabolically engineered
RT   Saccharomyces cerevisiae via an integrated strategy.";
RL   Microb. Cell Fact. 18:95-95(2019).
CC   -!- FUNCTION: This enzyme is required for electron transfer from NADP to
CC       cytochrome P450 in microsomes. It can also provide electron transfer to
CC       heme oxygenase and cytochrome B5. Reduces a variety of substrates in
CC       vitro, such as cytochrome c, feericyanide and dichloroindophenol.
CC       {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:10208644,
CC       ECO:0000269|PubMed:9235908, ECO:0000269|PubMed:9449848,
CC       ECO:0000269|PubMed:9880378, ECO:0000269|PubMed:9990323}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC         reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC         COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03212};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03212, ECO:0000269|PubMed:9990323};
CC       Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03212, ECO:0000269|PubMed:9990323};
CC       Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.2 uM for NADPH (at pH 7.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
CC         ECO:0000269|PubMed:9990323};
CC         KM=21.9 uM for NADPH (at pH 7.7 and 28 degrees Celsius)
CC         {ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
CC         ECO:0000269|PubMed:9990323};
CC         KM=2 uM for NADPH (at pH 7.25 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
CC         ECO:0000269|PubMed:9990323};
CC         KM=17 uM for cytochrome c (at pH 7.0 and 25 degrees Celsius)
CC         {ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
CC         ECO:0000269|PubMed:9990323};
CC         KM=24.3 uM for cytochrome c (at pH 7.7 and 28 degrees Celsius)
CC         {ECO:0000269|PubMed:9449848, ECO:0000269|PubMed:9880378,
CC         ECO:0000269|PubMed:9990323};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_03212}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9SB48-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques. {ECO:0000269|PubMed:9449848}.
CC   -!- BIOTECHNOLOGY: Saccharomyces cerevisiae expressing Glycyrrhiza
CC       uralensis CYP88D6 and CYP72A154, combined with the expression of
CC       Arabidopsis thaliana beta-amyrin synthase (beta-AS) and NADPH-
CC       cytochrome P450 reductase 1 (ATR1), accumulates glycyrrhetinic acid
CC       (GA) and, to lower levels, beta-amyrin; these GA production was
CC       increased in the presence of G.uralensis cytochrome b5 (CYB5).
CC       {ECO:0000269|PubMed:31138208}.
CC   -!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family. {ECO:0000255|HAMAP-Rule:MF_03212}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family. {ECO:0000255|HAMAP-
CC       Rule:MF_03212}.
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DR   EMBL; X66016; CAA46814.1; -; mRNA.
DR   EMBL; AL035356; CAA23011.1; -; Genomic_DNA.
DR   EMBL; AL161561; CAB79362.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84919.1; -; Genomic_DNA.
DR   EMBL; AY054688; AAK96879.1; -; mRNA.
DR   EMBL; BT008426; AAP37785.1; -; mRNA.
DR   PIR; T05582; T05582.
DR   RefSeq; NP_194183.1; NM_118585.4. [Q9SB48-1]
DR   AlphaFoldDB; Q9SB48; -.
DR   SMR; Q9SB48; -.
DR   BioGRID; 13843; 2.
DR   ComplexPortal; CPX-2833; Camalexin biosynthetic metabolon complex.
DR   IntAct; Q9SB48; 16.
DR   STRING; 3702.Q9SB48; -.
DR   iPTMnet; Q9SB48; -.
DR   PaxDb; 3702-AT4G24520-1; -.
DR   ProteomicsDB; 251284; -. [Q9SB48-1]
DR   EnsemblPlants; AT4G24520.1; AT4G24520.1; AT4G24520. [Q9SB48-1]
DR   GeneID; 828554; -.
DR   Gramene; AT4G24520.1; AT4G24520.1; AT4G24520. [Q9SB48-1]
DR   KEGG; ath:AT4G24520; -.
DR   Araport; AT4G24520; -.
DR   TAIR; AT4G24520; ATR1.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_001570_17_3_1; -.
DR   InParanoid; Q9SB48; -.
DR   OMA; YIQELWA; -.
DR   OrthoDB; 276396at2759; -.
DR   PhylomeDB; Q9SB48; -.
DR   BioCyc; ARA:AT4G24520-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G24520-MONOMER; -.
DR   BRENDA; 1.6.2.4; 399.
DR   SABIO-RK; Q9SB48; -.
DR   PRO; PR:Q9SB48; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9SB48; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:TAIR.
DR   GO; GO:0009698; P:phenylpropanoid metabolic process; IDA:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR   CDD; cd06204; CYPOR; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_03212; NCPR; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001094; Flavdoxin-like.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR023208; P450R.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR19384:SF111; NADPH--CYTOCHROME P450 REDUCTASE 1; 1.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF000208; P450R; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF52218; Flavoproteins; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   Genevisible; Q9SB48; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Endoplasmic reticulum; FAD;
KW   Flavoprotein; FMN; Membrane; NADP; Oxidoreductase;
KW   Phenylpropanoid metabolism; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..692
FT                   /note="NADPH--cytochrome P450 reductase 1"
FT                   /id="PRO_0000416839"
FT   TOPO_DOM        2..26
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   TOPO_DOM        48..692
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   DOMAIN          85..235
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   DOMAIN          290..537
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         91..96
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         146..149
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         184..193
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         219
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         310
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         470..473
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         488..490
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         504..507
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         551
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         612..613
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         618..622
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         654
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   BINDING         692
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         249
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862"
FT   CONFLICT        161
FT                   /note="Y -> S (in Ref. 1; CAA46814)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        477..480
FT                   /note="SPRL -> CQDW (in Ref. 1; CAA46814)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   692 AA;  76766 MW;  7DD77E418CCF2FA6 CRC64;
     MTSALYASDL FKQLKSIMGT DSLSDDVVLV IATTSLALVA GFVVLLWKKT TADRSGELKP
     LMIPKSLMAK DEDDDLDLGS GKTRVSIFFG TQTGTAEGFA KALSEEIKAR YEKAAVKVID
     LDDYAADDDQ YEEKLKKETL AFFCVATYGD GEPTDNAARF YKWFTEENER DIKLQQLAYG
     VFALGNRQYE HFNKIGIVLD EELCKKGAKR LIEVGLGDDD QSIEDDFNAW KESLWSELDK
     LLKDEDDKSV ATPYTAVIPE YRVVTHDPRF TTQKSMESNV ANGNTTIDIH HPCRVDVAVQ
     KELHTHESDR SCIHLEFDIS RTGITYETGD HVGVYAENHV EIVEEAGKLL GHSLDLVFSI
     HADKEDGSPL ESAVPPPFPG PCTLGTGLAR YADLLNPPRK SALVALAAYA TEPSEAEKLK
     HLTSPDGKDE YSQWIVASQR SLLEVMAAFP SAKPPLGVFF AAIAPRLQPR YYSISSSPRL
     APSRVHVTSA LVYGPTPTGR IHKGVCSTWM KNAVPAEKSH ECSGAPIFIR ASNFKLPSNP
     STPIVMVGPG TGLAPFRGFL QERMALKEDG EELGSSLLFF GCRNRQMDFI YEDELNNFVD
     QGVISELIMA FSREGAQKEY VQHKMMEKAA QVWDLIKEEG YLYVCGDAKG MARDVHRTLH
     TIVQEQEGVS SSEAEAIVKK LQTEGRYLRD VW
//