NCPR_RAT
ID NCPR_RAT Reviewed; 678 AA.
AC P00388;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
DE Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
DE EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
GN Name=Por {ECO:0000255|HAMAP-Rule:MF_03212};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3919392; DOI=10.1073/pnas.82.4.973;
RA Porter T.D., Kasper C.B.;
RT "Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase
RT cDNA and identification of flavin-binding domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:973-977(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3082610; DOI=10.1089/dna.1986.5.1;
RA Murakami H., Yabusaki Y., Ohkawa H.;
RT "Expression of rat NADPH-cytochrome P-450 reductase cDNA in Saccharomyces
RT cerevisiae.";
RL DNA 5:1-10(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=2125483; DOI=10.1021/bi00494a009;
RA Porter T.D., Beck T.W., Kasper C.B.;
RT "NADPH-cytochrome P-450 oxidoreductase gene organization correlates with
RT structural domains of the protein.";
RL Biochemistry 29:9814-9818(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 64-678 IN COMPLEX WITH FAD; FMN
RP AND NADP.
RX PubMed=9237990; DOI=10.1073/pnas.94.16.8411;
RA Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S.S., Kim J.-J.P.;
RT "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype
RT for FMN- and FAD-containing enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8411-8416(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 57-678 IN COMPLEX WITH FAD; FMN
RP AND NADP.
RX PubMed=11371558; DOI=10.1074/jbc.m101731200;
RA Hubbard P.A., Shen A.L., Paschke R., Kasper C.B., Kim J.-J.P.;
RT "NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and
RT electron transfer.";
RL J. Biol. Chem. 276:29163-29170(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 57-678 IN COMPLEX WITH FAD; FMN
RP AND NADP.
RX PubMed=19171935; DOI=10.1074/jbc.m807868200;
RA Hamdane D., Xia C., Im S.C., Zhang H., Kim J.J., Waskell L.;
RT "Structure and function of an NADPH-cytochrome P450 oxidoreductase in an
RT open conformation capable of reducing cytochrome P450.";
RL J. Biol. Chem. 284:11374-11384(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 57-678.
RX PubMed=21345800; DOI=10.1074/jbc.m111.230532;
RA Xia C., Hamdane D., Shen A.L., Choi V., Kasper C.B., Pearl N.M., Zhang H.,
RA Im S.C., Waskell L., Kim J.J.;
RT "Conformational changes of NADPH-cytochrome P450 oxidoreductase are
RT essential for catalysis and cofactor binding.";
RL J. Biol. Chem. 286:16246-16260(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (4.30 ANGSTROMS) OF 58-678 IN COMPLEX WITH FAD; FMN
RP AND NADP.
RA Sugishima M., Sato H., Higashimoto Y., Harada J., Wada K., Fukuyama K.,
RA Noguchi M.;
RT "Structural basis for the electron transfer from an open form of NADPH-
RT cytochrome P450 oxidoreductase to heme oxygenase.";
RL Submitted (OCT-2013) to the PDB data bank.
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. {ECO:0000255|HAMAP-Rule:MF_03212}.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9237990};
CC Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9237990};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9237990};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
CC ECO:0000269|PubMed:9237990};
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 -!- 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; M10068; AAA41064.1; -; mRNA.
DR EMBL; M12516; AAA41067.1; -; mRNA.
DR EMBL; M58937; AAA41683.1; -; Genomic_DNA.
DR EMBL; M58932; AAA41683.1; JOINED; Genomic_DNA.
DR EMBL; M58933; AAA41683.1; JOINED; Genomic_DNA.
DR EMBL; M58934; AAA41683.1; JOINED; Genomic_DNA.
DR EMBL; M58935; AAA41683.1; JOINED; Genomic_DNA.
DR EMBL; M58936; AAA41683.1; JOINED; Genomic_DNA.
DR PIR; A36073; RDRTO4.
DR RefSeq; NP_113764.1; NM_031576.1.
DR PDB; 1AMO; X-ray; 2.60 A; A/B=64-678.
DR PDB; 1J9Z; X-ray; 2.70 A; A/B=57-676.
DR PDB; 1JA0; X-ray; 2.60 A; A/B=57-676.
DR PDB; 1JA1; X-ray; 1.80 A; A/B=57-678.
DR PDB; 3ES9; X-ray; 3.40 A; A/B/C=57-678.
DR PDB; 3OJW; X-ray; 2.20 A; A=57-678.
DR PDB; 3OJX; X-ray; 2.50 A; A=57-678.
DR PDB; 3WKT; X-ray; 4.30 A; A/B=58-678.
DR PDB; 4Y7C; X-ray; 2.20 A; A/B=57-678.
DR PDB; 4Y9R; X-ray; 2.40 A; A/B=57-678.
DR PDB; 4Y9U; X-ray; 1.95 A; A/B=57-678.
DR PDB; 4YAF; X-ray; 1.91 A; A/B=57-678.
DR PDB; 4YAL; X-ray; 1.88 A; A/B=57-678.
DR PDB; 4YAO; X-ray; 2.50 A; A/B=57-678.
DR PDB; 4YAU; X-ray; 2.20 A; A/B=57-678.
DR PDB; 4YAW; X-ray; 2.00 A; A/B=57-678.
DR PDB; 5URD; X-ray; 1.90 A; A/B=57-678.
DR PDB; 5URE; X-ray; 2.30 A; A/B=57-678.
DR PDB; 5URG; X-ray; 2.30 A; A/B=57-678.
DR PDB; 5URH; X-ray; 2.50 A; A/B=57-678.
DR PDB; 5URI; X-ray; 2.70 A; A/B=57-678.
DR PDB; 6J79; X-ray; 3.33 A; A/B=59-678.
DR PDB; 6J7A; X-ray; 3.27 A; A/B=59-678.
DR PDB; 6J7I; X-ray; 3.30 A; A/B=59-678.
DR PDB; 6NJR; X-ray; 2.70 A; A/B=57-678.
DR PDB; 7L18; X-ray; 2.54 A; AAA/BBB=57-678.
DR PDBsum; 1AMO; -.
DR PDBsum; 1J9Z; -.
DR PDBsum; 1JA0; -.
DR PDBsum; 1JA1; -.
DR PDBsum; 3ES9; -.
DR PDBsum; 3OJW; -.
DR PDBsum; 3OJX; -.
DR PDBsum; 3WKT; -.
DR PDBsum; 4Y7C; -.
DR PDBsum; 4Y9R; -.
DR PDBsum; 4Y9U; -.
DR PDBsum; 4YAF; -.
DR PDBsum; 4YAL; -.
DR PDBsum; 4YAO; -.
DR PDBsum; 4YAU; -.
DR PDBsum; 4YAW; -.
DR PDBsum; 5URD; -.
DR PDBsum; 5URE; -.
DR PDBsum; 5URG; -.
DR PDBsum; 5URH; -.
DR PDBsum; 5URI; -.
DR PDBsum; 6J79; -.
DR PDBsum; 6J7A; -.
DR PDBsum; 6J7I; -.
DR PDBsum; 6NJR; -.
DR PDBsum; 7L18; -.
DR AlphaFoldDB; P00388; -.
DR SMR; P00388; -.
DR BioGRID; 248088; 1.
DR IntAct; P00388; 1.
DR STRING; 10116.ENSRNOP00000001961; -.
DR ChEMBL; CHEMBL2817; -.
DR iPTMnet; P00388; -.
DR PhosphoSitePlus; P00388; -.
DR jPOST; P00388; -.
DR PaxDb; P00388; -.
DR PRIDE; P00388; -.
DR Ensembl; ENSRNOT00000101964; ENSRNOP00000078537; ENSRNOG00000001442.
DR GeneID; 29441; -.
DR KEGG; rno:29441; -.
DR UCSC; RGD:68335; rat.
DR CTD; 5447; -.
DR RGD; 68335; Por.
DR eggNOG; KOG1158; Eukaryota.
DR GeneTree; ENSGT00940000156847; -.
DR HOGENOM; CLU_001570_17_3_1; -.
DR InParanoid; P00388; -.
DR OMA; QKRYQRD; -.
DR OrthoDB; 318396at2759; -.
DR PhylomeDB; P00388; -.
DR TreeFam; TF105719; -.
DR BioCyc; MetaCyc:MON-14290; -.
DR BRENDA; 1.6.2.4; 5301.
DR SABIO-RK; P00388; -.
DR EvolutionaryTrace; P00388; -.
DR PRO; PR:P00388; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001442; Expressed in lung and 19 other tissues.
DR Genevisible; P00388; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:RGD.
DR GO; GO:0009055; F:electron transfer activity; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IMP:RGD.
DR GO; GO:0010181; F:FMN binding; IMP:RGD.
DR GO; GO:0016787; F:hydrolase activity; IDA:RGD.
DR GO; GO:0047726; F:iron-cytochrome-c reductase activity; IDA:RGD.
DR GO; GO:0050661; F:NADP binding; IDA:RGD.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:BHF-UCL.
DR GO; GO:0008941; F:nitric oxide dioxygenase activity; IDA:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; IEP:RGD.
DR GO; GO:0090346; P:cellular organofluorine metabolic process; ISO:RGD.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
DR GO; GO:0071371; P:cellular response to gonadotropin stimulus; IEP:RGD.
DR GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
DR GO; GO:0070988; P:demethylation; IDA:RGD.
DR GO; GO:0022900; P:electron transport chain; ISO:RGD.
DR GO; GO:0019395; P:fatty acid oxidation; IDA:RGD.
DR GO; GO:0009812; P:flavonoid metabolic process; IEP:RGD.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
DR GO; GO:0060192; P:negative regulation of lipase activity; IDA:RGD.
DR GO; GO:0043602; P:nitrate catabolic process; IDA:RGD.
DR GO; GO:0046210; P:nitric oxide catabolic process; IDA:RGD.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IMP:RGD.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:RGD.
DR GO; GO:0032770; P:positive regulation of monooxygenase activity; ISO:RGD.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:RGD.
DR GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IDA:RGD.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:RGD.
DR GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IMP:RGD.
DR GO; GO:0071548; P:response to dexamethasone; IDA:RGD.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 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 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; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endoplasmic reticulum; FAD; Flavoprotein; FMN;
KW Membrane; NADP; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P16435"
FT CHAIN 2..678
FT /note="NADPH--cytochrome P450 reductase"
FT /id="PRO_0000167600"
FT TOPO_DOM 2..22
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT TOPO_DOM 44..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 80..224
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT DOMAIN 279..521
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
FT BINDING 86..91
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 138..141
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 173..182
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 208
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:21345800,
FT ECO:0000269|PubMed:9237990"
FT BINDING 298
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990"
FT BINDING 424
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|Ref.8"
FT BINDING 454..457
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 472..474
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8"
FT BINDING 478
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 488..491
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 535
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 596..597
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 602..606
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT BINDING 639
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990"
FT BINDING 677
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03212,
FT ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935,
FT ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990,
FT ECO:0000269|Ref.8"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P16435"
FT CONFLICT 255
FT /note="V -> A (in Ref. 3; AAA41683)"
FT /evidence="ECO:0000305"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 150..158
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 212..231
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 266..270
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:5URD"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:5URG"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 383..389
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:3OJX"
FT HELIX 396..403
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 420..424
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 427..433
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 468..474
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 489..496
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 508..514
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 534..537
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 538..552
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 560..567
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 576..584
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 587..595
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 598..601
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 605..611
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 626..632
FT /evidence="ECO:0007829|PDB:1JA1"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 636..651
FT /evidence="ECO:0007829|PDB:1JA1"
FT HELIX 656..668
FT /evidence="ECO:0007829|PDB:1JA1"
FT STRAND 671..677
FT /evidence="ECO:0007829|PDB:1JA1"
SQ SEQUENCE 678 AA; 76963 MW; AF3087E4D7A352D6 CRC64;
MGDSHEDTSA TMPEAVAEEV SLFSTTDMVL FSLIVGVLTY WFIFRKKKEE IPEFSKIQTT
APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA
DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH
FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES
SIRQYELVVH EDMDVAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTANR KLNQGTERHL
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQIGEILGA DLDVIMSLNN LDEESNKKHP
FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV
VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA
KSGRVNKGVA TSWLRAKEPA GENGGRALVP MFVRKSQFRL PFKSTTPVIM VGPGTGIAPF
MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA
HKVYVQHLLK RDREHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV
DYVKKLMTKG RYSLDVWS
