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 27-MAR-2024, entry version 211. 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}. 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; 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 PDB; 7U9S; X-ray; 2.10 A; A/B=1-347. DR PDB; 7U9U; X-ray; 1.66 A; A/B=1-347. DR PDB; 8HY5; X-ray; 2.10 A; A/B=1-347. 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 PDBsum; 7U9S; -. DR PDBsum; 7U9U; -. DR PDBsum; 8HY5; -. 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; 9606-ENSP00000228476; -. DR PeptideAtlas; P14920; -. DR ProteomicsDB; 53094; -. DR TopDownProteomics; P14920; -. DR Antibodypedia; 30788; 315 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 AGR; HGNC:2671; -. 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; 5359at2759; -. DR PhylomeDB; P14920; -. DR TreeFam; TF313887; -. DR BioCyc; MetaCyc:HS03351-MONOMER; -. 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; 13 hits in 1151 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 97 other cell types or tissues. DR ExpressionAtlas; P14920; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005782; C:peroxisomal matrix; 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; IDA:UniProtKB. 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:0007586; P:digestion; ISS:UniProtKB. DR GO; GO:0042416; P:dopamine biosynthetic process; IDA:UniProtKB. DR GO; GO:0006562; P:proline catabolic process; IDA:UniProtKB. DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR006181; D-amino_acid_oxidase_CS. DR InterPro; IPR023209; DAO. DR InterPro; IPR006076; FAD-dep_OxRdtase. DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1. DR PANTHER; PTHR11530:SF15; D-AMINO-ACID OXIDASE; 1. DR Pfam; PF01266; DAO; 1. DR PIRSF; PIRSF000189; D-aa_oxidase; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51971; Nucleotide-binding domain; 1. DR PROSITE; PS00677; DAO; 1. DR Genevisible; P14920; HS. 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:7U9U" FT HELIX 10..23 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 26..28 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 31..37 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:3G3E" FT HELIX 44..47 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 63..76 FT /evidence="ECO:0007829|PDB:7U9U" FT TURN 77..80 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 84..87 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 89..100 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 106..109 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 111..116 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 119..122 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 129..139 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 141..154 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 158..161 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 167..172 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 176..180 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 183..188 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 196..206 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 212..216 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 228..231 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 233..239 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 253..266 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 268..272 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 274..285 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 290..298 FT /evidence="ECO:0007829|PDB:7U9U" FT STRAND 301..309 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 312..314 FT /evidence="ECO:0007829|PDB:7U9U" FT HELIX 315..338 FT /evidence="ECO:0007829|PDB:7U9U" 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 //