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O31616 (GLOX_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine. Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine. Does not act on L-amino acids and other D-amino acids. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate. Ref.2 Ref.4

Catalytic activity

Glycine + H2O + O2 = glyoxylate + NH3 + H2O2. Ref.2 Ref.6

D-alanine + H2O + O2 = pyruvate + NH3 + H2O2. Ref.2 Ref.6

Sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2. Ref.2 Ref.6

N-ethylglycine + H2O + O2 = glyoxylate + ethylamine + H2O2. Ref.2 Ref.6

Cofactor

Binds 1 FAD per subunit.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis. Ref.4

Subunit structure

Homotetramer. Ref.2 Ref.4 Ref.5 Ref.6

Subcellular location

Cytoplasm Probable.

Disruption phenotype

Cells lacking this gene have an absolute requirement for the thiazole alcohol for growth. Ref.4

Biotechnological use

Introducing the gene coding for the glycine oxidase mutant Ser-51/Arg-54/Ala-244 in plants is an effective alternative mechanism for glyphosate tolerance in transgenic crops. In addition, transgenic plants that are able to oxidize glyphosate may represent an innovative bioremediation system for the soil treated with this herbicide. Ref.6

Sequence similarities

Belongs to the DAO family.

Biophysicochemical properties

Kinetic parameters:

KM=0.22 mM for sarcosine (at pH 8) Ref.2 Ref.6

KM=0.66 mM for N-ethylglycine (at pH 8)

KM=0.99 mM for glycine (at pH 8)

KM=46 mM for D-proline (at pH 8)

KM=81 mM for D-alanine (at pH 8)

KM=87 mM for glyphosate

pH dependence:

Optimum pH is 8.0.

Temperature dependence:

Optimum temperature is 45 degrees Celsius.

Ontologies

Keywords
   Biological processHerbicide resistance
Thiamine biosynthesis
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processresponse to herbicide

Inferred from electronic annotation. Source: UniProtKB-KW

thiamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

glycine oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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

Experimental info

Mutagenesis511G → R: 130-fold decrease in catalytic efficiency on glycine and 28-fold increase in that on glyphosate. Ref.6
Mutagenesis511G → S: 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with R-54 and A-244. Ref.6
Mutagenesis541A → R: 20-fold decrease in catalytic efficiency on glycine and 34-fold increase in that on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and A-244. Ref.6
Mutagenesis2441H → A: 2-fold decrease in catalytic efficiency on glycine and similar catalytic efficiency on glyphosate. 60-fold decrease in catalytic efficiency on glycine and 210-fold increase in that on glyphosate; when associated with S-51 and R-54. Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O31616 [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

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: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
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, FUNCTION IN THIAMINE BIOSYNTHESIS, PATHWAY, DISRUPTION PHENOTYPE, 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.
[6]"Glyphosate resistance by engineering the flavoenzyme glycine oxidase."
Pedotti M., Rosini E., Molla G., Moschetti T., Savino C., Vallone B., Pollegioni L.
J. Biol. Chem. 284:36415-36423(2009) [PubMed: 19864430] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF MUTANT SER-51/ARG-54/ALA-244 IN COMPLEX WITH GLYCOLATE AND FAD, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, SUBUNIT, BIOTECHNOLOGY, MUTAGENESIS OF GLY-51; ALA-54 AND HIS-244.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL009126 Genomic DNA. Translation: CAB13024.1.
PIRB69845.
RefSeqNP_389049.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NG3X-ray2.60A/B1-369[»]
1NG4X-ray2.30A/B1-369[»]
1RYIX-ray1.80A/B/C/D1-367[»]
3IF9X-ray2.60A/B/C/D1-369[»]
ProteinModelPortalO31616.
SMRO31616. Positions 1-364.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000004030; EBBACP00000004030; EBBACG00000004022.
GeneID939377.
GenomeReviewsGene locus BSU11670 in contig AL009126_GR.
KEGGbsu:BSU11670.
NMPDRfig|224308.1.peg.1168.
PATRIC18974051. VBIBacSub10457_1219.

Organism-specific databases

GenoListBSU11670. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001490.
HOGENOMHBG729204.
OMADVHVEPY.
PhylomeDBO31616.
ProtClustDBCLSK887074.

Enzyme and pathway databases

BioCycBSUB:BSU11670-MONOMER.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR012727. Gly_oxidase_ThiO.
[Graphical view]
KOK03153.
PfamPF01266. DAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR02352. Thiamin_ThiO. 1 hit.
ProtoNetSearch...

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: January 25, 2012
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents