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Reviewed, UniProtKB/Swiss-Prot O31616 (GLOX_BACSU)

Last modified June 16, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glycine oxidase
    EC=1.4.3.19
Gene names
Name: goxB
Synonyms: yjbR
Ordered Locus Names: BSU11670
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This deaminating oxidase catalyzes the oxidation of sarcosine (N-methylglycine), N-ethylglycine and glycine. Lower activities on D-alanine, D-valine, and D-proline are detected. Does not act on L-amino acids and other D-amino acids.

Catalytic activity

Glycine + H2O + O2 = glyoxylate + NH3 + H2O2.

D-alanine + H2O + O2 = pyruvate + NH3 + H2O2.

Sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2.

N-ethylglycine + H2O + O2 = glyoxylate + ethylamine + H2O2.

Cofactor

FAD.

Subunit structure

Homotetramer. Ref.4 Ref.5

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the DAMOX/DASOX family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 45 degrees Celsius.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionFAD binding

Inferred from electronic annotation. Source: InterPro

glycine oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Glycine oxidase
PRO_0000162773

Regions

Nucleotide binding7 – 2115FAD
Nucleotide binding34 – 352FAD
Nucleotide binding42 – 432FAD
Nucleotide binding47 – 493FAD
Nucleotide binding327 – 3337FAD

Sites

Binding site551Substrate
Binding site1741FAD; via amide nitrogen and carbonyl oxygen
Binding site3021Substrate
Binding site3291Substrate

Secondary structure

1 ............................................................. 369
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O31616-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7A9466117AC0A76A

FASTA36940,937
        10         20         30         40         50         60 
MKRHYEAVVI GGGIIGSAIA YYLAKENKNT ALFESGTMGG RTTSAAAGML GAHAECEERD 

        70         80         90        100        110        120 
AFFDFAMHSQ RLYKGLGEEL YALSGVDIRQ HNGGMFKLAF SEEDVLQLRQ MDDLDSVSWY 

       130        140        150        160        170        180 
SKEEVLEKEP YASGDIFGAS FIQDDVHVEP YFVCKAYVKA AKMLGAEIFE HTPVLHVERD 

       190        200        210        220        230        240 
GEALFIKTPS GDVWANHVVV ASGVWSGMFF KQLGLNNAFL PVKGECLSVW NDDIPLTKTL 

       250        260        270        280        290        300 
YHDHCYIVPR KSGRLVVGAT MKPGDWSETP DLGGLESVMK KAKTMLPAIQ NMKVDRFWAG 

       310        320        330        340        350        360 
LRPGTKDGKP YIGRHPEDSR ILFAAGHFRN GILLAPATGA LISDLIMNKE VNQDWLHAFR 


IDRKEAVQI

« Hide

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References

« Hide 'large scale' references
[1]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[2]"Purification and characterization of a novel glycine oxidase from Bacillus subtilis."
Nishiya Y., Imanaka T.
FEBS Lett. 438:263-266(1998) [PubMed: 9827558] [Abstract]
Cited for: CHARACTERIZATION.
Strain: MT-2.
[3]"Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein."
Job V., Marcone G.L., Pilone M.S., Pollegioni L.
J. Biol. Chem. 277:6985-6993(2002) [PubMed: 11744710] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis."
Settembre E.C., Dorrestein P.C., Park J.-H., Augustine A.M., Begley T.P., Ealick S.E.
Biochemistry 42:2971-2981(2003) [PubMed: 12627963] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FAD AND N-ACETYLGLYCINE, SUBUNIT.
[5]"Structure-function correlation in glycine oxidase from Bacillus subtilis."
Moertl M., Diederichs K., Welte W., Molla G., Motteran L., Andriolo G., Pilone M.S., Pollegioni L.
J. Biol. Chem. 279:29718-29727(2004) [PubMed: 15105420] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH GLYCOLATE AND FAD, SUBUNIT.

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Cross-references

Sequence databases

AL009126 Genomic DNA. Translation: CAB13024.1.
PIRB69845.
RefSeqNP_389049.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1NG3X-ray2.60A/B1-369[»]
1NG4X-ray2.30A/B1-369[»]
1RYIX-ray1.80A/B/C/D1-367[»]
ModBaseSearch...

Genome annotation databases

GeneID939377.
GenomeReviewsGene locus BSU11670 in contig AL009126_GR.
KEGGbsu:BSU11670.
NMPDRfig|224308.1.peg.1168.

Organism-specific databases

SubtiListBG13147. goxB. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMO31616.
OMAO31616. FAAGHFR.

Enzyme and pathway databases

BioCycBSUB224308:BSU1168-MON.
BRENDA1.4.3.19. 150.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR012727. Gly_oxidase_ThiO.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR02352. thiamin_ThiO. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameGLOX_BACSU
AccessionPrimary (citable) accession number: O31616
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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