NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=M-0718 / FERM P-2688;
PubMed=1982443 [NCBI, ExPASy, EBI, Israel, Japan]
Isogai T., Ono H., Ishitani Y., Kojo H., Ueda Y., Kohsaka M.;
"Structure and expression of cDNA for D-amino acid oxidase active against cephalosporin C from Fusarium solani.";
J. Biochem. 108:1063-1069(1990).

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.
SUBCELLULAR LOCATION: Peroxisome (Potential).
PTM: The N-terminus is blocked.
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

D00809; BAA00692.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JX0152; JX0152.

3D structure databases

HSSP

P80324; 1C0P. [HSSP ENTRY / PDB]

ModBase

P24552.

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

Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 361`	`361`	`D-amino-acid oxidase.`	`PRO_0000162766`
`NP_BIND`	`5 19`	`15`	`FAD (Potential).`
`MOTIF`	`359 361`	`3`	`Microbody targeting signal (Potential).`
`ACT_SITE`	`242 242`		`By similarity.`
`ACT_SITE`	`327 327`		`By similarity.`

Sequence information

Length: 361 AA [This is the length of the unprocessed precursor]

Molecular weight: 39696 Da [This is the MW of the unprocessed precursor]

CRC64: 148119480E2A67A5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNTIVVVGA GVIGLTSALL LSKNKGNKIT VVAKHMPGDY DVEYASPFAG ANHSPMATEE 

        70         80         90        100        110        120 
SSEWERRTWY EFKRLVEEVP EAGVHFQKSR IQRRNVDTEK AQRSGFPDAL FSKEPWFKNM 

       130        140        150        160        170        180 
FEDFREQHPS EVIPGYDSGC EFTSVCINTA IYLPWLLGQC IKNGVIVKRA ILNDISEAKK 

       190        200        210        220        230        240 
LSHAGKTPNI IVNATGLGSY KLGGVEDKTM APARGQIVVV RNESSPMLLT SGVEDGGADV 

       250        260        270        280        290        300 
MYLMQRAAGG GTILGGTYDV GNWESQPDPN IANRIMQRIV EVRPEIANGK GVKGLSVIRH 

       310        320        330        340        350        360 
AVGMRPWRKD GVRIEEEKLD DETWIVHNYG HSGWGYQGSY GCAENVVQLV DKVGKAAKSK 


L

P24552 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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