P80324 (OXDA_RHOTO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D-amino-acid oxidase
Short name=DAAO
Short name=DAMOX
Short name=DAO
EC=1.4.3.3

Gene names

Name:

DAO1

Organism

Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis)

Taxonomic identifier

5286 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Basidiomycota › Pucciniomycotina › Microbotryomycetes › Sporidiobolales › Rhodosporidium

Protein attributes

Sequence length	368 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme can effectively convert cephalosporin C into 7-beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid.
Catalytic activity	A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.
Cofactor	FAD.
Subunit structure	Homodimer.
Subcellular location	Peroxisome Potential.
Sequence similarities	Belongs to the DAMOX/DASOX family.

Ontologies

Keywords
Cellular component	Peroxisome
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular_component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	D-amino-acid oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 368

368

D-amino-acid oxidase

PRO_0000162767

Regions

Nucleotide binding

7 – 21

15

FAD

Nucleotide binding

35 – 36

2

FAD

Nucleotide binding

47 – 48

2

FAD

Nucleotide binding

52 – 54

3

FAD

Nucleotide binding

334 – 338

5

FAD

Motif

366 – 368

3

Microbody targeting signal Potential

Sites

Binding site

162

1

FAD; via amide nitrogen and carbonyl oxygen

Binding site

179

1

FAD

Binding site

223

1

Substrate

Binding site

285

1

Substrate

Binding site

335

1

Substrate; via carbonyl oxygen

Binding site

339

1

FAD; via amide nitrogen

Secondary structure

1

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368

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

14 – 25

12

Beta strand

29 – 36

8

Helix

48 – 50

3

Turn

61 – 63

3

Helix

65 – 81

17

Turn

82 – 85

4

Beta strand

86 – 99

14

Helix

100 – 106

7

Turn

107 – 111

5

Beta strand

116 – 118

3

Helix

120 – 122

3

Beta strand

128 – 136

9

Helix

139 – 152

14

Beta strand

156 – 159

4

Helix

165 – 167

3

Beta strand

173 – 177

5

Helix

180 – 184

5

Beta strand

194 – 205

12

Beta strand

212 – 214

3

Beta strand

222 – 227

6

Turn

228 – 230

3

Beta strand

231 – 235

5

Helix

249 – 262

14

Helix

264 – 266

3

Beta strand

267 – 271

5

Helix

272 – 274

3

Beta strand

276 – 288

13

Beta strand

293 – 302

10

Turn

305 – 307

3

Beta strand

323 – 331

9

Helix

334 – 336

3

Helix

337 – 359

23

Sequences

	Sequence		Length	Mass (Da)
	P80324 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 99940118BCFA886E	FASTA	368	40,076
	10 20 30 40 50 60 MHSQKRVVVL GSGVIGLSSA LILARKGYSV HILARDLPED VSSQTFASPW AGANWTPFMT 70 80 90 100 110 120 LTDGPRQAKW EESTFKKWVE LVPTGHAMWL KGTRRFAQNE DGLLGHWYKD ITPNYRPLPS 130 140 150 160 170 180 SECPPGAIGV TYDTLSVHAP KYCQYLAREL QKLGATFERR TVTSLEQAFD GADLVVNATG 190 200 210 220 230 240 LGAKSIAGID DQAAEPIRGQ TVLVKSPCKR CTMDSSDPAS PAYIIPRPGG EVICGGTYGV 250 260 270 280 290 300 GDWDLSVNPE TVQRILKHCL RLDPTISSDG TIEGIEVLRH NVGLRPARRG GPRVEAERIV 310 320 330 340 350 360 LPLDRTKSPL SLGRGSARAA KEKEVTLVHA YGFSSAGYQQ SWGAAEDVAQ LVDEAFQRYH GAARESKL

References

[1]	"The primary structure of D-amino acid oxidase from Rhodotorula gracilis." Faotto L., Pollegioni L., Ceciliani F., Ronchi S., Pilone M.S. Biotechnol. Lett. 17:193-198(1995) Cited for: PROTEIN SEQUENCE.
[2]	Pilone M.S., Pollegioni L., Molla G., Campaner S., Martegani E. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 26217 / Pan.
[3]	"D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217." Alonso J., Barredo J.L., Diez B., Salto F., Garcia J.L., Cortes E. Microbiology 144:1095-1101(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26217 / Pan.
[4]	Liaw G.J., Lee Y.J., Lee Y.H., Chen L.L., Chu W.S. Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 10788 / CBS 14 / IAM 13469 / JCM 10020 / NBRC 0559 / NRRL Y-1091.
[5]	"Studies on the structural and functional aspects of Rhodotorula gracilis D-amino acid oxidase by limited trypsinolysis." Pollegioni L., Ceciliani F., Curti B., Ronchi S., Pilone M.S. Biochem. J. 310:577-583(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[6]	"The X-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation." Umhau S., Pollegioni L., Molla G., Diederichs K., Welte W., Pilone M.S., Ghisla S. Proc. Natl. Acad. Sci. U.S.A. 97:12463-12468(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 1-361 IN COMPLEXES WITH FAD; D-ALANINE; 2-AMINOBENZOIC ACID AND LACTATE, ENZYME MECHANISM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U60066 mRNA. Translation: AAB51107.1.
Z71657 Genomic DNA. Translation: CAA96323.1.
AF003339 mRNA. Translation: AAB93974.1.
AF003340 Genomic DNA. Translation: AAB93975.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1C0I	X-ray	1.90	A	1-361	[»]
1C0K	X-ray	1.46	A	1-361	[»]
1C0L	X-ray	1.73	A	1-361	[»]
1C0P	X-ray	1.20	A	1-361	[»]
2DZG	model	-	@	1-368	[»]

ProteinModelPortal

P80324.

SMR

P80324. Positions 1-361.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P80324.

Family and domain databases

InterPro

IPR023209. D-aa_oxidase.
IPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
[Graphical view]

PANTHER

PTHR11530. PTHR11530. 1 hit.

Pfam

PF01266. DAO. 1 hit.
[Graphical view]

PIRSF

PIRSF000189. D-aa_oxidase. 1 hit.

PROSITE

PS00677. DAO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P80324.

Entry information

Entry name

OXDA_RHOTO

Accession

Primary (citable) accession number: P80324

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program