OXDA_RHOTO
ID OXDA_RHOTO Reviewed; 368 AA.
AC P80324;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=D-amino-acid oxidase;
DE Short=DAAO;
DE Short=DAMOX;
DE Short=DAO;
DE EC=1.4.3.3;
GN Name=DAO1;
OS Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=5286;
RN [1]
RP PROTEIN SEQUENCE.
RA Faotto L., Pollegioni L., Ceciliani F., Ronchi S., Pilone M.S.;
RT "The primary structure of D-amino acid oxidase from Rhodotorula gracilis.";
RL Biotechnol. Lett. 17:193-198(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 26217 / Pan;
RA Pilone M.S., Pollegioni L., Molla G., Campaner S., Martegani E.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26217 / Pan;
RX PubMed=9579082; DOI=10.1099/00221287-144-4-1095;
RA Alonso J., Barredo J.L., Diez B., Salto F., Garcia J.L., Cortes E.;
RT "D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium
RT toruloides) ATCC 26217.";
RL Microbiology 144:1095-1101(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10788 / CBS 14 / BCRC 20306 / IAM 13469 / JCM 10020 / NBRC 0559
RC / NRRL Y-1091;
RA Liaw G.J., Lee Y.J., Lee Y.H., Chen L.L., Chu W.S.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP CHARACTERIZATION.
RX PubMed=7654197; DOI=10.1042/bj3100577;
RA Pollegioni L., Ceciliani F., Curti B., Ronchi S., Pilone M.S.;
RT "Studies on the structural and functional aspects of Rhodotorula gracilis
RT D-amino acid oxidase by limited trypsinolysis.";
RL Biochem. J. 310:577-583(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 1-361 IN COMPLEXES WITH FAD;
RP D-ALANINE; 2-AMINOBENZOIC ACID AND LACTATE, AND ENZYME MECHANISM.
RX PubMed=11070076; DOI=10.1073/pnas.97.23.12463;
RA Umhau S., Pollegioni L., Molla G., Diederichs K., Welte W., Pilone M.S.,
RA Ghisla S.;
RT "The X-ray structure of D-amino acid oxidase at very high resolution
RT identifies the chemical mechanism of flavin-dependent substrate
RT dehydrogenation.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12463-12468(2000).
CC -!- FUNCTION: This enzyme can effectively convert cephalosporin C into 7-
CC beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DAMOX/DASOX family. {ECO:0000305}.
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DR EMBL; U60066; AAB51107.1; -; mRNA.
DR EMBL; Z71657; CAA96323.1; -; Genomic_DNA.
DR EMBL; AF003339; AAB93974.1; -; mRNA.
DR EMBL; AF003340; AAB93975.1; -; Genomic_DNA.
DR PDB; 1C0I; X-ray; 1.90 A; A=1-361.
DR PDB; 1C0K; X-ray; 1.46 A; A=1-361.
DR PDB; 1C0L; X-ray; 1.73 A; A=1-361.
DR PDB; 1C0P; X-ray; 1.20 A; A=1-361.
DR PDBsum; 1C0I; -.
DR PDBsum; 1C0K; -.
DR PDBsum; 1C0L; -.
DR PDBsum; 1C0P; -.
DR AlphaFoldDB; P80324; -.
DR SMR; P80324; -.
DR BRENDA; 1.4.3.3; 5424.
DR SABIO-RK; P80324; -.
DR EvolutionaryTrace; P80324; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
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; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Peroxisome.
FT CHAIN 1..368
FT /note="D-amino-acid oxidase"
FT /id="PRO_0000162767"
FT MOTIF 366..368
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 7..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 47..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 52..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 223
FT /ligand="substrate"
FT BINDING 285
FT /ligand="substrate"
FT BINDING 334..338
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 335
FT /ligand="substrate"
FT BINDING 339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1C0P"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:1C0P"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 86..99
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:1C0P"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1C0L"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 194..205
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1C0P"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 249..262
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 276..288
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:1C0P"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1C0P"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1C0P"
FT HELIX 337..359
FT /evidence="ECO:0007829|PDB:1C0P"
SQ SEQUENCE 368 AA; 40076 MW; 99940118BCFA886E CRC64;
MHSQKRVVVL GSGVIGLSSA LILARKGYSV HILARDLPED VSSQTFASPW AGANWTPFMT
LTDGPRQAKW EESTFKKWVE LVPTGHAMWL KGTRRFAQNE DGLLGHWYKD ITPNYRPLPS
SECPPGAIGV TYDTLSVHAP KYCQYLAREL QKLGATFERR TVTSLEQAFD GADLVVNATG
LGAKSIAGID DQAAEPIRGQ TVLVKSPCKR CTMDSSDPAS PAYIIPRPGG EVICGGTYGV
GDWDLSVNPE TVQRILKHCL RLDPTISSDG TIEGIEVLRH NVGLRPARRG GPRVEAERIV
LPLDRTKSPL SLGRGSARAA KEKEVTLVHA YGFSSAGYQQ SWGAAEDVAQ LVDEAFQRYH
GAARESKL
