Monomeric sarcosine oxidase - Bacillus sp. (strain B-0618)

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Reviewed, UniProtKB/Swiss-Prot P40859 (MSOX_BACB0)

Last modified June 16, 2009. Version 76. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    Monomeric sarcosine oxidase
      Short name=MSOX
    EC=1.5.3.1

Gene names

Name:	soxA
Synonyms:	sox

Organism

Bacillus sp. (strain B-0618)

Taxonomic identifier

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the oxidative demethylation of sarcosine. Can also oxidize other secondary amino acids such as N-methyl-L-alanine. HAMAP MF_00516
Catalytic activity	Sarcosine + H₂O + O₂ = glycine + formaldehyde + H₂O₂. HAMAP MF_00516
Cofactor	Binds 1 FAD per subunit. HAMAP MF_00516
Enzyme regulation	Pyrrole-2-carboxylate is a competitive inhibitor. N-(cyclopropyl)glycine (CPG) is a mechanism-based inhibitor and inactivates the enzyme by covalently modifying the flavin. HAMAP MF_00516
Subunit structure	Monomer. HAMAP MF_00516
Subcellular location	Cytoplasm. HAMAP MF_00516
Sequence similarities	Belongs to the MSOX/MTOX family. MSOX subfamily.
Mass spectrometry	Molecular mass is 43839 Da from positions 1 - 390. Determined by ESI. Ref.3

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tetrahydrofolate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	sarcosine oxidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

390

Monomeric sarcosine oxidase HAMAP MF_00516

PRO_0000213762

Regions

Nucleotide binding

31

FAD Potential

Amino acid modifications

Modified residue

1

S-8alpha-FAD cysteine HAMAP MF_00516

Secondary structure

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390

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P40859-1 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: D830491B80230BCF
Show »

390

43,182

        10         20         30         40         50         60 
MSTHFDVIVV GAGSMGMAAG YQLAKQGVKT LLVDAFDPPH TNGSHHGDTR IIRHAYGEGR 

        70         80         90        100        110        120 
EYVPLALRSQ ELWYELEKET HHKIFTKTGV LVFGPKGESA FVAETMEAAK EHSLTVDLLE 

       130        140        150        160        170        180 
GDEINKRWPG ITVPENYNAI FEPNSGVLFS ENCIRAYREL AEARGAKVLT HTRVEDFDIS 

       190        200        210        220        230        240 
PDSVKIETAN GSYTADKLIV SMGAWNSKLL SKLNLDIPLQ PYRQVVGFFE SDESKYSNDI 

       250        260        270        280        290        300 
DFPGFMVEVP NGIYYGFPSF GGCGLKLGYH TFGQKIDPDT INREFGVYPE DESNLRAFLE 

       310        320        330        340        350        360 
EYMPGANGEL KRGAVCMYTK TLDEHFIIDL HPEHSNVVIA AGFSGHGFKF SSGVGEVLSQ 

       370        380        390 
LALTGKTEHD ISIFSINRPA LKESLQKTTI

References

[1]	"Cloning, sequencing, overexpression in Escherichia coil of a sarcosine oxidase-encoding gene linked to the Bacillus creatinase gene." Suzuki K., Sagai H., Imamura S., Sugiyama M. J. Ferment. Bioeng. 77:231-234(1994) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Suzuki K. Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 117.
[3]	"Structure of the flavocoenzyme of two homologous amine oxidases: monomeric sarcosine oxidase and N-methyltryptophan oxidase." Wagner M.A., Khanna P., Jorns M.S. Biochemistry 38:5588-5595(1999) [PubMed: 10220347] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 313-319, MASS SPECTROMETRY.
[4]	"Monomeric sarcosine oxidase: 2. Kinetic studies with sarcosine, alternate substrates, and a substrate analogue." Wagner M.A., Jorns M.S. Biochemistry 39:8825-8829(2000) [PubMed: 10913293] [Abstract] Cited for: CHARACTERIZATION.
[5]	"Inactivation of monomeric sarcosine oxidase by reaction with N-(cyclopropyl)glycine." Zhao G., Qu J., Davis F.A., Jorns M.S. Biochemistry 39:14341-14347(2000) [PubMed: 11087383] [Abstract] Cited for: CHARACTERIZATION.
[6]	"Monomeric sarcosine oxidase: structure of a covalently flavinylated amine oxidizing enzyme." Trickey P., Wagner M.A., Jorns M.S., Mathews F.S. Structure 7:331-345(1999) [PubMed: 10368302] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

D16521 Genomic DNA. Translation: BAA03967.1.

PIR

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EL5	X-ray	1.80	A/B	2-390	[»]
1EL7	X-ray	1.90	A/B	2-390	[»]
1EL8	X-ray	1.90	A/B	2-390	[»]
1EL9	X-ray	2.00	A/B	2-390	[»]
1ELI	X-ray	2.00	A/B	2-390	[»]
1L9C	X-ray	1.90	A/B	2-390	[»]
1L9D	X-ray	1.95	A/B	2-390	[»]
1L9E	X-ray	1.85	A/B	2-390	[»]
2A89	X-ray	1.85	A/B	2-390	[»]
2GB0	X-ray	1.85	A/B	2-390	[»]
2GF3	X-ray	1.30	A/B	2-390	[»]
3BHF	X-ray	2.10	A/B	1-390	[»]
3BHK	X-ray	1.71	A/B	1-390	[»]

ModBase

Family and domain databases

HAMAP

MF_00516.
[Tree]

InterPro

IPR006076. FAD-dep_OxRdtase.
IPR006281. SoxA_mon.
[Graphical view]

Pfam

PF01266. DAO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01377. soxA_mon. 1 hit.

ProtoNet

Entry information

Entry name

MSOX_BACB0

Accession

Primary (citable) accession number: P40859

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents