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Protein

Monomeric sarcosine oxidase

Gene

soxA

Organism
Bacillus sp. (strain NS-129)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative demethylation of sarcosine.By similarity

Catalytic activityi

Sarcosine + H2O + O2 = glycine + formaldehyde + H2O2.

Cofactori

FADNote: Binds 1 FAD per subunit.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 3631FADSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Monomeric sarcosine oxidase (EC:1.5.3.1)
Short name:
MSOX
Gene namesi
Name:soxA
OrganismiBacillus sp. (strain NS-129)
Taxonomic identifieri1419 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Monomeric sarcosine oxidasePRO_0000213761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei316 – 3161S-8alpha-FAD cysteine

Expressioni

Inductioni

By sarcosine.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi14 – 2411Combined sources
Turni25 – 273Combined sources
Beta strandi30 – 334Combined sources
Beta strandi41 – 455Combined sources
Beta strandi47 – 526Combined sources
Helixi62 – 7918Combined sources
Beta strandi90 – 956Combined sources
Helixi100 – 11112Combined sources
Beta strandi117 – 1204Combined sources
Helixi122 – 1276Combined sources
Beta strandi137 – 1426Combined sources
Beta strandi146 – 1494Combined sources
Helixi150 – 16314Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi174 – 1796Combined sources
Beta strandi184 – 1885Combined sources
Beta strandi191 – 20010Combined sources
Helixi203 – 2053Combined sources
Helixi206 – 2094Combined sources
Helixi210 – 2134Combined sources
Beta strandi220 – 22910Combined sources
Helixi233 – 2364Combined sources
Helixi238 – 2403Combined sources
Beta strandi244 – 2496Combined sources
Beta strandi252 – 2576Combined sources
Beta strandi265 – 2717Combined sources
Turni278 – 2803Combined sources
Helixi290 – 30213Combined sources
Helixi304 – 3063Combined sources
Beta strandi310 – 32011Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi337 – 3415Combined sources
Helixi348 – 3503Combined sources
Helixi351 – 36414Combined sources
Helixi372 – 3743Combined sources
Helixi379 – 3813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZOVX-ray1.86A/B2-387[»]
ProteinModelPortaliP23342.
SMRiP23342. Positions 2-382.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23342.

Family & Domainsi

Sequence similaritiesi

Belongs to the MSOX/MTOX family. MSOX subfamily.Curated

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
HAMAPiMF_00516. MSOX.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR006281. SoxA_mon.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01377. soxA_mon. 1 hit.

Sequencei

Sequence statusi: Complete.

P23342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTHFDVIVV GAGSMGMAAG YYLAKQGVKT LLVDSFDPPH TNGSHHGDTR
60 70 80 90 100
IIRHAYGEGR EYVPFALRAQ ELWYELEKET HHKIFTQTGV LVYGPKGGSA
110 120 130 140 150
FVSETMEAAN IHSLEHELFE GKQLTDRWAG VEVPDNYEAI FEPNSGVLFS
160 170 180 190 200
ENCIQAYREL AEAHGATVLT YTPVEDFEVT EDLVTIKTAK GSYTANKLVV
210 220 230 240 250
SMGAWNSKLL SKLDVEIPLQ PYRQVVGFFE CDEAKYSNNA HYPAFMVEVE
260 270 280 290 300
NGIYYGFPSF GGSGLKIGYH SYGQQIDPDT INREFGAYPE DEANLRKFLE
310 320 330 340 350
QYMPGANGEL KKGAVCMYTK TPDEHFVIDL HPKYSNVAIA AGFSGHGFKF
360 370 380
SSVVGETLAQ LATTGKTEHD ISIFSLNRDA LKKEAVK
Length:387
Mass (Da):42,873
Last modified:November 1, 1991 - v1
Checksum:i7A960CC422841F98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10553 Genomic DNA. Translation: BAA01410.1.
PIRiJU0461.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10553 Genomic DNA. Translation: BAA01410.1.
PIRiJU0461.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZOVX-ray1.86A/B2-387[»]
ProteinModelPortaliP23342.
SMRiP23342. Positions 2-382.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23342.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
HAMAPiMF_00516. MSOX.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR006281. SoxA_mon.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01377. soxA_mon. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and expression of the sarcosine oxidase gene from Bacillus sp. NS-129 in Escherichia coli."
    Koyama Y., Yamamoto-Otake H., Suzuki M., Nakano E.
    Agric. Biol. Chem. 55:1259-1263(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-34.
  2. "Crystal structure of monomeric sarcosine oxidase from Bacillus sp. NS-129 reveals multiple conformations at the active-site loop."
    Nagata K., Sasaki H., Ohtsuka J., Hua M., Okai M., Kubota K., Kamo M., Ito K., Ichikawa T., Koyama Y., Tanokura M.
    Proc. Jpn. Acad. 81:220-224(2005)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-387 IN COMPLEX WITH FAD.

Entry informationi

Entry nameiMSOX_BACSN
AccessioniPrimary (citable) accession number: P23342
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 11, 2015
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.