[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Testis; NIH - Mammalian Gene Collection (MGC) project; Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Metabolizes sarcosine, L-pipecolic acid and L-proline (By similarity).
CATALYTIC ACTIVITY: Sarcosine + H₂O + O₂ = glycine + formaldehyde + H₂O₂.
CATALYTIC ACTIVITY: L-pipecolate + O₂ = 2,3,4,5-tetrahydropyridine-2-carboxylate + H₂O₂.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Monomer (By similarity).
SUBCELLULAR LOCATION: Peroxisome (By similarity).
SIMILARITY: Belongs to the MSOX/MTOX 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

BT020944; AAX08961.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC114006; AAI14007.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001014878.2; -.

UniGene

Bt.38917

3D structure databases

ModBase

Q29RU9.

Ontologies

GO:0050031;	Molecular function: L-pipecolate oxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR006076; FAD-dep_OxRdtase.
IPR006281; SoxA_mon.
Graphical view of domain structure.

Pfam

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

TIGRFAMs

TIGR01377; soxA_mon; 1.

BLOCKS

Q29RU9.

Genome annotation databases

Ensembl

ENSBTAG00000007946; Bos taurus. [Contig view]

GeneID

509102; -.

KEGG

bta:509102; -.

Phylogenomic databases

HOVERGEN

Q29RU9; -.

Other

ProtoNet

Q29RU9.

UniRef

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

Keywords

FAD; Flavoprotein; Oxidoreductase; Peroxisome.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 392`	`392`	`Peroxisomal sarcosine oxidase.`	`PRO_0000244375`
`NP_BIND`	`9 39`	`31`	`FAD (Potential).`
`MOTIF`	`390 392`	`3`	`Microbody targeting signal (Potential).`
`MOD_RES`	`321 321`		`S-8alpha-FAD cysteine (By similarity).`
`CONFLICT`	`161 161`		`A -> G (in Ref. 2; AAI14007).`

Sequence information

Length: 392 AA [This is the length of the unprocessed precursor]

Molecular weight: 43820 Da [This is the MW of the unprocessed precursor]

CRC64: E62446943F200F67 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAAQRELYDA IVIGAGIQGC FTAYHLAKHS KKVLLLEQFF LPHSRGSSHG QSRIIRRAYP 

        70         80         90        100        110        120 
EDFYTQMMAE CYSLWAQLEH EAGTQLYRQT GLLLLGMKEN PELKIIQATL SRQGVEHQCL 

       130        140        150        160        170        180 
SSEELKQRFP NIRLARGEVG LLEVSGGVLY ADKALRALQD AIRQLGGIVH DGEKVVEIKS 

       190        200        210        220        230        240 
GLPVMVKTTS RSYQAKSLII TAGPWTNRLL RPLGAELPLQ TLRINVCYWQ EKVPGSYSVS 

       250        260        270        280        290        300 
QAFPCFMGLG LSLAPHHIYG LPSREYPGLM KVCYHHGNNA DPEERDCPAA FSDIQDVHIL 

       310        320        330        340        350        360 
SGFVRDHLPD LQPEPAVMEH CMYTNTPDGH FVLDRHPKYD NIVIGAGFSG HGFKLSPVVG 

       370        380        390 
KILYELSMKL TPSYDLTPFR ISRFPSLGKA HL

Q29RU9 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