OXDA_HUMAN
ID OXDA_HUMAN Reviewed; 347 AA.
AC P14920; B2R7I5; Q16758; Q8N6R2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=D-amino-acid oxidase;
DE Short=DAAO;
DE Short=DAMOX;
DE Short=DAO;
DE EC=1.4.3.3;
GN Name=DAO; Synonyms=DAMOX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=2901986; DOI=10.1016/0014-5793(88)80252-7;
RA Momoi K., Fukui K., Watanabe F., Miyake Y.;
RT "Molecular cloning and sequence analysis of cDNA encoding human kidney D-
RT amino acid oxidase.";
RL FEBS Lett. 238:180-184(1988).
RN [2]
RP SEQUENCE REVISION.
RA Momoi K.;
RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Colon, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
RX PubMed=1356107; DOI=10.1016/s0021-9258(19)37007-3;
RA Fukui K., Miyake Y.;
RT "Molecular cloning and chromosomal localization of a human gene encoding D-
RT amino-acid oxidase.";
RL J. Biol. Chem. 267:18631-18638(1992).
RN [7]
RP INVOLVEMENT IN SCZD, AND INTERACTION WITH DAOA.
RX PubMed=12364586; DOI=10.1073/pnas.182412499;
RA Chumakov I., Blumenfeld M., Guerassimenko O., Cavarec L., Palicio M.,
RA Abderrahim H., Bougueleret L., Barry C., Tanaka H., La Rosa P., Puech A.,
RA Tahri N., Cohen-Akenine A., Delabrosse S., Lissarrague S., Picard F.-P.,
RA Maurice K., Essioux L., Millasseau P., Grel P., Debailleul V., Simon A.-M.,
RA Caterina D., Dufaure I., Malekzadeh K., Belova M., Luan J.-J., Bouillot M.,
RA Sambucy J.-L., Primas G., Saumier M., Boubkiri N., Martin-Saumier S.,
RA Nasroune M., Peixoto H., Delaye A., Pinchot V., Bastucci M., Guillou S.,
RA Chevillon M., Sainz-Fuertes R., Meguenni S., Aurich-Costa J., Cherif D.,
RA Gimalac A., Van Duijn C., Gauvreau D., Ouellette G., Fortier I.,
RA Raelson J., Sherbatich T., Riazanskay N., Rogaev E., Raeymaekers P.,
RA Aerssens J., Konings F., Luyten W., Macciardi F., Sham P.C., Straub R.E.,
RA Weinberger D.R., Cohen N., Cohen D.;
RT "Genetic and physiological data implicating the new human gene G72 and the
RT gene for D-amino acid oxidase in schizophrenia.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13675-13680(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FAD AND THE INHIBITOR
RP BENZOATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17088322; DOI=10.1110/ps.062421606;
RA Kawazoe T., Tsuge H., Pilone M.S., Fukui K.;
RT "Crystal structure of human D-amino acid oxidase: context-dependent
RT variability of the backbone conformation of the VAAGL hydrophobic stretch
RT located at the si-face of the flavin ring.";
RL Protein Sci. 15:2708-2717(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEXES WITH FAD AND
RP IMINO-SERINE; IMINO-DOPA AND O-AMINOBENZOATE, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND FUNCTION.
RX PubMed=17303072; DOI=10.1016/j.bbrc.2007.01.181;
RA Kawazoe T., Tsuge H., Imagawa T., Aki K., Kuramitsu S., Fukui K.;
RT "Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative
RT pathway for dopamine biosynthesis.";
RL Biochem. Biophys. Res. Commun. 355:385-391(2007).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH FAD AND SYNTHETIC
RP INHIBITOR.
RX PubMed=18455394; DOI=10.1016/j.bmcl.2008.04.020;
RA Sparey T., Abeywickrema P., Almond S., Brandon N., Byrne N., Campbell A.,
RA Hutson P.H., Jacobson M., Jones B., Munshi S., Pascarella D., Pike A.,
RA Prasad G.S., Sachs N., Sakatis M., Sardana V., Venkatraman S., Young M.B.;
RT "The discovery of fused pyrrole carboxylic acids as novel, potent D-amino
RT acid oxidase (DAO) inhibitors.";
RL Bioorg. Med. Chem. Lett. 18:3386-3391(2008).
CC -!- FUNCTION: Regulates the level of the neuromodulator D-serine in the
CC brain. Has high activity towards D-DOPA and contributes to dopamine
CC synthesis. Could act as a detoxifying agent which removes D-amino acids
CC accumulated during aging. Acts on a variety of D-amino acids with a
CC preference for those having small hydrophobic side chains followed by
CC those bearing polar, aromatic, and basic groups. Does not act on acidic
CC amino acids. {ECO:0000269|PubMed:17303072}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59871; EC=1.4.3.3;
CC Evidence={ECO:0000269|PubMed:17088322};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 mM for D-serine {ECO:0000269|PubMed:17088322,
CC ECO:0000269|PubMed:17303072};
CC KM=1.7 mM for D-proline {ECO:0000269|PubMed:17088322,
CC ECO:0000269|PubMed:17303072};
CC KM=1.1 mM for D-tyrosine {ECO:0000269|PubMed:17088322,
CC ECO:0000269|PubMed:17303072};
CC KM=1.5 mM for D-DOPA {ECO:0000269|PubMed:17088322,
CC ECO:0000269|PubMed:17303072};
CC KM=1.2 mM for D-phenylalanine {ECO:0000269|PubMed:17088322,
CC ECO:0000269|PubMed:17303072};
CC KM=0.9 mM for D-alanine {ECO:0000269|PubMed:17088322,
CC ECO:0000269|PubMed:17303072};
CC -!- SUBUNIT: Homodimer (PubMed:17088322, PubMed:18455394). Interacts with
CC DAOA (PubMed:12364586). {ECO:0000269|PubMed:12364586,
CC ECO:0000269|PubMed:17088322, ECO:0000269|PubMed:18455394}.
CC -!- INTERACTION:
CC P14920; O43741: PRKAB2; NbExp=6; IntAct=EBI-3908043, EBI-1053424;
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial
CC psychotic disorder or group of disorders characterized by disturbances
CC in the form and content of thought (e.g. delusions, hallucinations), in
CC mood (e.g. inappropriate affect), in sense of self and relationship to
CC the external world (e.g. loss of ego boundaries, withdrawal), and in
CC behavior (e.g bizarre or apparently purposeless behavior). Although it
CC affects emotions, it is distinguished from mood disorders in which such
CC disturbances are primary. Similarly, there may be mild impairment of
CC cognitive function, and it is distinguished from the dementias in which
CC disturbed cognitive function is considered primary. Some patients
CC manifest schizophrenic as well as bipolar disorder symptoms and are
CC often given the diagnosis of schizoaffective disorder.
CC {ECO:0000269|PubMed:12364586}. Note=Disease susceptibility may be
CC associated with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR EMBL; X13227; CAA31614.1; -; mRNA.
DR EMBL; AK312995; BAG35832.1; -; mRNA.
DR EMBL; CH471054; EAW97837.1; -; Genomic_DNA.
DR EMBL; BC029057; AAH29057.1; -; mRNA.
DR EMBL; BC074770; AAH74770.1; -; mRNA.
DR EMBL; D11370; BAA20974.1; -; Genomic_DNA.
DR CCDS; CCDS9122.1; -.
DR PIR; S01340; S01340.
DR RefSeq; NP_001908.3; NM_001917.4.
DR RefSeq; XP_011536306.1; XM_011538004.2.
DR RefSeq; XP_011536307.1; XM_011538005.2.
DR PDB; 2DU8; X-ray; 2.50 A; A/B/G/J=1-347.
DR PDB; 2E48; X-ray; 2.90 A; A/B/C/D=1-347.
DR PDB; 2E49; X-ray; 3.20 A; A/B/C/D=1-347.
DR PDB; 2E4A; X-ray; 2.60 A; A/B/C/D=1-347.
DR PDB; 2E82; X-ray; 2.70 A; A/B/C/D=1-347.
DR PDB; 3CUK; X-ray; 2.49 A; A/B/C/D=1-347.
DR PDB; 3G3E; X-ray; 2.20 A; A/B/C/D=1-347.
DR PDB; 3W4I; X-ray; 2.50 A; A/B/C/D=1-347.
DR PDB; 3W4J; X-ray; 2.74 A; A/B/C/D=1-347.
DR PDB; 3W4K; X-ray; 2.86 A; A/B/C/D=1-347.
DR PDB; 3ZNN; X-ray; 1.90 A; A/B=1-347.
DR PDB; 3ZNO; X-ray; 2.30 A; A/B=1-347.
DR PDB; 3ZNP; X-ray; 2.40 A; A/B=1-347.
DR PDB; 3ZNQ; X-ray; 2.75 A; A/B=1-347.
DR PDB; 4QFC; X-ray; 2.40 A; A/B=1-347.
DR PDB; 4QFD; X-ray; 2.85 A; A/B=1-347.
DR PDB; 5ZJ9; X-ray; 2.60 A; A/B/C/D=1-340.
DR PDB; 5ZJA; X-ray; 2.60 A; A/B/C/D=1-340.
DR PDB; 6KBP; X-ray; 2.25 A; A/B/C/D=1-338.
DR PDBsum; 2DU8; -.
DR PDBsum; 2E48; -.
DR PDBsum; 2E49; -.
DR PDBsum; 2E4A; -.
DR PDBsum; 2E82; -.
DR PDBsum; 3CUK; -.
DR PDBsum; 3G3E; -.
DR PDBsum; 3W4I; -.
DR PDBsum; 3W4J; -.
DR PDBsum; 3W4K; -.
DR PDBsum; 3ZNN; -.
DR PDBsum; 3ZNO; -.
DR PDBsum; 3ZNP; -.
DR PDBsum; 3ZNQ; -.
DR PDBsum; 4QFC; -.
DR PDBsum; 4QFD; -.
DR PDBsum; 5ZJ9; -.
DR PDBsum; 5ZJA; -.
DR PDBsum; 6KBP; -.
DR AlphaFoldDB; P14920; -.
DR SMR; P14920; -.
DR BioGRID; 107980; 11.
DR IntAct; P14920; 5.
DR STRING; 9606.ENSP00000228476; -.
DR BindingDB; P14920; -.
DR ChEMBL; CHEMBL5485; -.
DR DrugBank; DB07979; (2E)-3-(3,4-DIHYDROXYPHENYL)-2-IMINOPROPANOIC ACID.
DR DrugBank; DB02838; 3,4-Dihydro-2h-Pyrrolium-5-Carboxylate.
DR DrugBank; DB04166; Anthranilic acid.
DR DrugBank; DB03793; Benzoic acid.
DR DrugBank; DB03225; D-Tryptophan.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03531; Flavin-adenine dinucleotide-N5-isobutyl ketone.
DR DrugBank; DB02988; Imino-Tryptophan.
DR DrugCentral; P14920; -.
DR iPTMnet; P14920; -.
DR PhosphoSitePlus; P14920; -.
DR BioMuta; DAO; -.
DR DMDM; 25453448; -.
DR MassIVE; P14920; -.
DR PaxDb; P14920; -.
DR PeptideAtlas; P14920; -.
DR PRIDE; P14920; -.
DR ProteomicsDB; 53094; -.
DR TopDownProteomics; P14920; -.
DR Antibodypedia; 30788; 299 antibodies from 31 providers.
DR DNASU; 1610; -.
DR Ensembl; ENST00000228476.8; ENSP00000228476.3; ENSG00000110887.8.
DR GeneID; 1610; -.
DR KEGG; hsa:1610; -.
DR MANE-Select; ENST00000228476.8; ENSP00000228476.3; NM_001917.5; NP_001908.3.
DR UCSC; uc001tnr.5; human.
DR CTD; 1610; -.
DR DisGeNET; 1610; -.
DR GeneCards; DAO; -.
DR HGNC; HGNC:2671; DAO.
DR HPA; ENSG00000110887; Group enriched (brain, kidney, liver).
DR MalaCards; DAO; -.
DR MIM; 124050; gene.
DR MIM; 181500; phenotype.
DR neXtProt; NX_P14920; -.
DR OpenTargets; ENSG00000110887; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR PharmGKB; PA27139; -.
DR VEuPathDB; HostDB:ENSG00000110887; -.
DR eggNOG; KOG3923; Eukaryota.
DR GeneTree; ENSGT00390000018635; -.
DR InParanoid; P14920; -.
DR OMA; LWWPYRI; -.
DR OrthoDB; 1363414at2759; -.
DR PhylomeDB; P14920; -.
DR TreeFam; TF313887; -.
DR BioCyc; MetaCyc:HS03351-MON; -.
DR BRENDA; 1.4.3.3; 2681.
DR PathwayCommons; P14920; -.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SABIO-RK; P14920; -.
DR SignaLink; P14920; -.
DR BioGRID-ORCS; 1610; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; DAO; human.
DR EvolutionaryTrace; P14920; -.
DR GenomeRNAi; 1610; -.
DR Pharos; P14920; Tchem.
DR PRO; PR:P14920; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P14920; protein.
DR Bgee; ENSG00000110887; Expressed in right lobe of liver and 96 other tissues.
DR ExpressionAtlas; P14920; baseline and differential.
DR Genevisible; P14920; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0055130; P:D-alanine catabolic process; IDA:UniProtKB.
DR GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
DR GO; GO:0036088; P:D-serine catabolic process; IDA:UniProtKB.
DR GO; GO:0070178; P:D-serine metabolic process; IDA:UniProtKB.
DR GO; GO:0042416; P:dopamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006562; P:proline catabolic process; IDA:UniProtKB.
DR InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; PTHR11530; 1.
DR Pfam; PF01266; DAO; 1.
DR PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR PROSITE; PS00677; DAO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Oxidoreductase; Peroxisome;
KW Reference proteome; Schizophrenia.
FT CHAIN 1..347
FT /note="D-amino-acid oxidase"
FT /id="PRO_0000162761"
FT MOTIF 345..347
FT /note="Microbody targeting signal"
FT BINDING 3..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17088322,
FT ECO:0000269|PubMed:18455394"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17088322,
FT ECO:0000269|PubMed:18455394"
FT BINDING 44..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17088322,
FT ECO:0000269|PubMed:18455394"
FT BINDING 49..51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17088322,
FT ECO:0000269|PubMed:18455394"
FT BINDING 53
FT /ligand="substrate"
FT BINDING 164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17088322,
FT ECO:0000269|PubMed:18455394"
FT BINDING 182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17088322,
FT ECO:0000269|PubMed:18455394"
FT BINDING 217
FT /ligand="substrate"
FT BINDING 228
FT /ligand="substrate"
FT BINDING 283
FT /ligand="substrate"
FT BINDING 312..317
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17088322,
FT ECO:0000269|PubMed:18455394"
FT BINDING 313
FT /ligand="substrate"
FT CONFLICT 31
FT /note="D -> H (in Ref. 1; CAA31614)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="R -> A (in Ref. 1; CAA31614)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3G3E"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:3ZNN"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:3ZNN"
FT TURN 106..110
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3ZNN"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 274..285
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 290..296
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:3ZNN"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:3ZNN"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:6KBP"
FT HELIX 315..336
FT /evidence="ECO:0007829|PDB:3ZNN"
SQ SEQUENCE 347 AA; 39474 MW; A508E603872F3072 CRC64;
MRVVVIGAGV IGLSTALCIH ERYHSVLQPL DIKVYADRFT PLTTTDVAAG LWQPYLSDPN
NPQEADWSQQ TFDYLLSHVH SPNAENLGLF LISGYNLFHE AIPDPSWKDT VLGFRKLTPR
ELDMFPDYGY GWFHTSLILE GKNYLQWLTE RLTERGVKFF QRKVESFEEV AREGADVIVN
CTGVWAGALQ RDPLLQPGRG QIMKVDAPWM KHFILTHDPE RGIYNSPYII PGTQTVTLGG
IFQLGNWSEL NNIQDHNTIW EGCCRLEPTL KNARIIGERT GFRPVRPQIR LEREQLRTGP
SNTEVIHNYG HGGYGLTIHW GCALEAAKLF GRILEEKKLS RMPPSHL
