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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)DescriptionActionsGraphical viewLength
Nucleotide bindingi6 – 36FADSequence analysisAdd BLAST31

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002137611 – 387Monomeric sarcosine oxidaseAdd BLAST387

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei316S-8alpha-FAD cysteine1

Expressioni

Inductioni

By sarcosine.

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

Secondary structure

1387
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi14 – 24Combined sources11
Turni25 – 27Combined sources3
Beta strandi30 – 33Combined sources4
Beta strandi41 – 45Combined sources5
Beta strandi47 – 52Combined sources6
Helixi62 – 79Combined sources18
Beta strandi90 – 95Combined sources6
Helixi100 – 111Combined sources12
Beta strandi117 – 120Combined sources4
Helixi122 – 127Combined sources6
Beta strandi137 – 142Combined sources6
Beta strandi146 – 149Combined sources4
Helixi150 – 163Combined sources14
Beta strandi167 – 169Combined sources3
Beta strandi174 – 179Combined sources6
Beta strandi184 – 188Combined sources5
Beta strandi191 – 200Combined sources10
Helixi203 – 205Combined sources3
Helixi206 – 209Combined sources4
Helixi210 – 213Combined sources4
Beta strandi220 – 229Combined sources10
Helixi233 – 236Combined sources4
Helixi238 – 240Combined sources3
Beta strandi244 – 249Combined sources6
Beta strandi252 – 257Combined sources6
Beta strandi265 – 271Combined sources7
Turni278 – 280Combined sources3
Helixi290 – 302Combined sources13
Helixi304 – 306Combined sources3
Beta strandi310 – 320Combined sources11
Beta strandi327 – 330Combined sources4
Beta strandi337 – 341Combined sources5
Helixi348 – 350Combined sources3
Helixi351 – 364Combined sources14
Helixi372 – 374Combined sources3
Helixi379 – 381Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZOVX-ray1.86A/B2-387[»]
ProteinModelPortaliP23342.
SMRiP23342.
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. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZOVX-ray1.86A/B2-387[»]
ProteinModelPortaliP23342.
SMRiP23342.
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. 1 hit.
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...

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 2, 2016
This is version 92 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.