Glycine oxidase

NameGlycine oxidase
Synonyms
  • 1.4.3.19
  • GO
  • goxB
  • yjbR
Gene NamethiO
OrganismBacillus subtilis (strain 168)
Amino acid sequence
>lcl|BSEQ0016486|Glycine oxidase
MKRHYEAVVIGGGIIGSAIAYYLAKENKNTALFESGTMGGRTTSAAAGMLGAHAECEERD
AFFDFAMHSQRLYKGLGEELYALSGVDIRQHNGGMFKLAFSEEDVLQLRQMDDLDSVSWY
SKEEVLEKEPYASGDIFGASFIQDDVHVEPYFVCKAYVKAAKMLGAEIFEHTPVLHVERD
GEALFIKTPSGDVWANHVVVASGVWSGMFFKQLGLNNAFLPVKGECLSVWNDDIPLTKTL
YHDHCYIVPRKSGRLVVGATMKPGDWSETPDLGGLESVMKKAKTMLPAIQNMKVDRFWAG
LRPGTKDGKPYIGRHPEDSRILFAAGHFRNGILLAPATGALISDLIMNKEVNQDWLHAFR
IDRKEAVQI
Number of residuesNone
Molecular Weight40936.53
Theoretical pI6.32
GO Classification
Functions
  • flavin adenine dinucleotide binding
  • glycine oxidase activity
Processes
  • response to herbicide
  • thiamine diphosphate biosynthetic process
  • thiamine biosynthetic process
Components
  • cytoplasm
General FunctionGlycine oxidase activity
Specific FunctionCatalyzes 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.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDO31616
UniProtKB Entry Name
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0016487|Glycine oxidase (thiO)
ATGAAAAGGCATTATGAAGCAGTGGTGATTGGAGGCGGAATTATCGGTTCCGCAATTGCT
TATTATTTGGCAAAGGAAAACAAAAACACCGCATTGTTTGAAAGCGGAACAATGGGCGGC
AGAACGACAAGTGCCGCTGCCGGAATGCTGGGCGCCCATGCCGAATGCGAGGAACGTGAC
GCGTTTTTTGATTTCGCTATGCACAGTCAGCGTCTGTACAAAGGTCTTGGAGAAGAGCTT
TATGCATTATCCGGTGTGGATATCAGGCAGCATAACGGCGGTATGTTTAAGCTTGCATTT
TCTGAAGAAGATGTGCTGCAGCTGAGACAGATGGACGATTTGGACTCTGTCAGCTGGTAT
TCAAAAGAAGAGGTGTTAGAAAAAGAGCCGTATGCGTCTGGTGACATCTTTGGTGCATCT
TTTATTCAGGATGATGTGCATGTGGAGCCTTATTTTGTTTGCAAGGCATATGTGAAAGCA
GCAAAAATGCTTGGGGCGGAGATTTTTGAGCATACGCCCGTCCTGCATGTCGAACGTGAC
GGTGAAGCCCTGTTCATCAAGACCCCTAGCGGAGACGTATGGGCTAATCATGTTGTCGTT
GCCAGCGGGGTGTGGAGCGGAATGTTTTTTAAACAGCTTGGACTGAACAATGCTTTTCTC
CCTGTAAAAGGGGAGTGCCTGTCCGTTTGGAATGATGATATCCCGCTGACAAAAACGCTT
TACCATGATCACTGCTATATCGTACCGAGAAAAAGCGGAAGACTGGTTGTCGGCGCGACA
ATGAAGCCGGGGGACTGGAGTGAAACACCGGATCTTGGCGGATTGGAATCTGTTATGAAA
AAAGCAAAAACGATGCTGCCGGCTATACAGAATATGAAGGTGGATCGTTTTTGGGCGGGA
CTCCGTCCGGGAACAAAGGATGGAAAACCGTACATCGGCAGACATCCTGAGGACAGCCGT
ATTTTATTTGCGGCTGGCCATTTCAGAAACGGGATCCTGCTTGCTCCCGCAACGGGCGCT
TTGATCAGTGATCTCATCATGAATAAAGAGGTCAACCAAGACTGGCTGCACGCATTCCGA
ATTGATCGCAAGGAGGCGGTTCAGATATGA
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC ID
Chromosome LocationNone
LocusNone
References
  1. Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Cordani JJ, Connerton IF, Cummings NJ, Daniel RA, Denziot F, Devine KM, Dusterhoft A, Ehrlich SD, Emmerson PT, Entian KD, Errington J, Fabret C, Ferrari E, Foulger D, Fritz C, Fujita M, Fujita Y, Fuma S, Galizzi A, Galleron N, Ghim SY, Glaser P, Goffeau A, Golightly EJ, Grandi G, Guiseppi G, Guy BJ, Haga K, Haiech J, Harwood CR, Henaut A, Hilbert H, Holsappel S, Hosono S, Hullo MF, Itaya M, Jones L, 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 SM, Levine A, Liu H, Masuda S, Mauel C, Medigue C, Medina N, Mellado RP, Mizuno M, Moestl D, Nakai S, Noback M, Noone D, O'Reilly M, Ogawa K, Ogiwara A, Oudega B, Park SH, Parro V, Pohl TM, Portelle D, Porwollik S, Prescott AM, 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 SJ, Serror P, Shin BS, Soldo B, Sorokin A, Tacconi E, Takagi T, Takahashi H, Takemaru K, Takeuchi M, Tamakoshi A, Tanaka T, Terpstra P, Togoni A, Tosato V, Uchiyama S, Vandebol M, Vannier F, Vassarotti A, Viari A, Wambutt R, Wedler H, Weitzenegger T, Winters P, Wipat A, Yamamoto H, Yamane K, Yasumoto K, Yata K, Yoshida K, Yoshikawa HF, Zumstein E, Yoshikawa H, Danchin A: The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature. 1997 Nov 20;390(6657):249-56. [9384377 ]
  2. Nishiya Y, Imanaka T: Purification and characterization of a novel glycine oxidase from Bacillus subtilis. FEBS Lett. 1998 Nov 6;438(3):263-6. [9827558 ]
  3. Job V, Marcone GL, Pilone MS, Pollegioni L: Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein. J Biol Chem. 2002 Mar 1;277(9):6985-93. Epub 2001 Dec 13. [11744710 ]
  4. Settembre EC, Dorrestein PC, Park JH, Augustine AM, Begley TP, Ealick SE: Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Biochemistry. 2003 Mar 18;42(10):2971-81. [12627963 ]
  5. Mortl M, Diederichs K, Welte W, Molla G, Motteran L, Andriolo G, Pilone MS, Pollegioni L: Structure-function correlation in glycine oxidase from Bacillus subtilis. J Biol Chem. 2004 Jul 9;279(28):29718-27. Epub 2004 Apr 22. [15105420 ]
  6. Pedotti M, Rosini E, Molla G, Moschetti T, Savino C, Vallone B, Pollegioni L: Glyphosate resistance by engineering the flavoenzyme glycine oxidase. J Biol Chem. 2009 Dec 25;284(52):36415-23. doi: 10.1074/jbc.M109.051631. Epub 2009 Oct 28. [19864430 ]

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