Reviewed, UniProtKB/Swiss-Prot P40859 (MSOX_BACB0)

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

69000 [NCBI]

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.
Catalytic activity	Sarcosine + H(2)O + O(2) = glycine + formaldehyde + H(2)O(2).
Cofactor	Binds 1 FAD per subunit.
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.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the MSOX/MTOX family. MSOX subfamily.
Mass spectrometry	Molecular weight 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: HAMAP
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

1 – 390

390

Monomeric sarcosine oxidase

PRO_0000213762

Regions

Nucleotide binding

6 – 36

31

FAD Potential

Amino acid modifications

Modified residue

316

1

S-8alpha-FAD cysteine

Secondary structure

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390

Helix Strand Turn

Details...

Beta strand

5 – 10

6

Helix

14 – 25

12

Beta strand

30 – 33

4

Beta strand

41 – 45

5

Beta strand

47 – 52

6

Helix

60 – 62

3

Helix

63 – 79

17

Beta strand

90 – 95

6

Helix

100 – 111

12

Beta strand

117 – 120

4

Helix

122 – 127

6

Beta strand

137 – 142

6

Beta strand

146 – 149

4

Helix

150 – 163

14

Beta strand

167 – 169

3

Beta strand

174 – 179

6

Beta strand

184 – 188

5

Beta strand

191 – 200

10

Helix

203 – 205

3

Helix

206 – 209

4

Helix

210 – 213

4

Beta strand

220 – 229

10

Helix

233 – 236

4

Helix

238 – 240

3

Beta strand

244 – 249

6

Beta strand

252 – 257

6

Beta strand

265 – 271

7

Turn

278 – 280

3

Helix

290 – 302

13

Helix

304 – 306

3

Beta strand

310 – 320

11

Beta strand

327 – 331

5

Beta strand

334 – 341

8

Helix

348 – 350

3

Helix

351 – 364

14

Helix

372 – 374

3

Helix

379 – 381

3

Sequences

	Sequence		Length	Mass (Da)
	P40859-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: D830491B80230BCF	FASTA	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

EMBLGenBankDDBJ

D16521 Genomic DNA. Translation: BAA03967.1.

PIR

I39975.

3D structure databases

PDBMSD

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

Search...

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

Search...

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:	November 25, 2008
This is version 75 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)