[1]	PROTEIN SEQUENCE. Faotto L., Pollegioni L., Ceciliani F., Ronchi S., Pilone M.S.; "The primary structure of D-amino acid oxidase from Rhodotorula gracilis."; Biotechnol. Lett. 17:193-198(1995).
[2]	NUCLEOTIDE SEQUENCE. STRAIN=ATCC 26217 / Pan; Pilone M.S., Pollegioni L., Molla G., Campaner S., Martegani E.; Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 26217 / Pan; PubMed=9579082 [NCBI, ExPASy, EBI, Israel, Japan] Alonso J., Barredo J.L., Diez B., Salto F., Garcia J.L., Cortes E.; "D-amino-acid oxidase gene from Rhodotorula gracilis (Rhodosporidium toruloides) ATCC 26217."; Microbiology 144:1095-1101(1998).
[4]	NUCLEOTIDE SEQUENCE. STRAIN=ATCC 10788 / CBS 14 / IFO 0559 / JCM 10020 / NRRL Y-1091; Liaw G.J., Lee Y.J., Lee Y.H., Chen L.L., Chu W.S.; Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[5]	CHARACTERIZATION. PubMed=7654197 [NCBI, ExPASy, EBI, Israel, Japan] Pollegioni L., Ceciliani F., Curti B., Ronchi S., Pilone M.S.; "Studies on the structural and functional aspects of Rhodotorula gracilis D-amino acid oxidase by limited trypsinolysis."; Biochem. J. 310:577-583(1995).

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: Homodimer.
SUBCELLULAR LOCATION: Peroxisome (Potential).
SIMILARITY: Belongs to the DAMOX/DASOX family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U60066; AAB51107.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71657; CAA96323.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF003339; AAB93974.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF003340; AAB93975.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1C0I; X-ray; 1.90 A; A=1-361.	[ExPASy / RCSB / EBI]
1C0K; X-ray; 1.46 A; A=1-361.	[ExPASy / RCSB / EBI]
1C0L; X-ray; 1.73 A; A=1-361.	[ExPASy / RCSB / EBI]
1C0P; X-ray; 1.20 A; A=1-361.	[ExPASy / RCSB / EBI]
2DZG; Model; -; @=1-368.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1C0I; -.
1C0K; -.
1C0L; -.
1C0P; -.
2DZG; -.

ModBase

P80324.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from electronic annotation from UniProtKB-KW).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0003884;	Molecular function: D-amino-acid oxidase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR006181; D-amino_acid_oxidase_CS.
IPR006076; FAD-dep_OxRdtase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF01266; DAO; 1.
Pfam graphical view of domain structure.

PS00677; DAO; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 368`	`368`	`D-amino-acid oxidase.`	`PRO_0000162767`
`NP_BIND`	`7 21`	`15`	`FAD (Potential).`
`MOTIF`	`366 368`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`223 223`		`By similarity.`
`ACT_SITE`	`329 329`		`By similarity.`
`STRAND`	`6 10`	`5`
`HELIX`	`14 25`	`12`
`STRAND`	`29 36`	`8`
`HELIX`	`48 50`	`3`
`TURN`	`61 63`	`3`
`HELIX`	`65 81`	`17`
`TURN`	`82 85`	`4`
`STRAND`	`86 99`	`14`
`HELIX`	`100 106`	`7`
`TURN`	`107 111`	`5`
`HELIX`	`120 122`	`3`
`STRAND`	`128 136`	`9`
`HELIX`	`139 152`	`14`
`STRAND`	`156 159`	`4`
`HELIX`	`165 167`	`3`
`STRAND`	`173 177`	`5`
`HELIX`	`180 184`	`5`
`STRAND`	`194 205`	`12`
`STRAND`	`212 216`	`5`
`STRAND`	`222 227`	`6`
`TURN`	`228 230`	`3`
`STRAND`	`231 235`	`5`
`HELIX`	`249 262`	`14`
`HELIX`	`264 266`	`3`
`STRAND`	`267 271`	`5`
`HELIX`	`272 274`	`3`
`STRAND`	`276 288`	`13`
`STRAND`	`293 302`	`10`
`TURN`	`305 307`	`3`
`STRAND`	`323 331`	`9`
`HELIX`	`337 359`	`23`

Sequence information

Length: 368 AA [This is the length of the unprocessed precursor]

Molecular weight: 40076 Da [This is the MW of the unprocessed precursor]

CRC64: 99940118BCFA886E [This is a checksum on the sequence]

        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

P80324 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools