GLYOX_PSEPK
ID GLYOX_PSEPK Reviewed; 365 AA.
AC Q88Q83;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Glycine oxidase {ECO:0000303|PubMed:26875494};
DE Short=GO {ECO:0000303|PubMed:26875494};
DE EC=1.4.3.19 {ECO:0000269|PubMed:26875494};
GN Name=thiO {ECO:0000303|PubMed:26875494, ECO:0000312|EMBL:AAN66238.1};
GN OrderedLocusNames=PP_0612 {ECO:0000312|EMBL:AAN66238.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBUNIT, AND PATHWAY.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=26875494; DOI=10.3177/jnsv.61.506;
RA Equar M.Y., Tani Y., Mihara H.;
RT "Purification and properties of glycine oxidase from Pseudomonas putida
RT KT2440.";
RL J. Nutr. Sci. Vitaminol. 61:506-510(2015).
CC -!- FUNCTION: Catalyzes the oxidation of glycine, leading to glyoxyl imine
CC and hydrogen peroxide as primary products; glyoxyl imine is used for
CC the biosynthesis of the thiazole ring of thiamine. Otherwise, glyoxyl
CC imine is spontaneously hydrolyzed in water to produce glyoxylate and
CC ammonia. Can also use sarcosine (N-methylglycine) as substrate, and, to
CC a lesser extent, N-ethylglycine and D-proline. Has no activity towards
CC other amino-acids D-Asp, D-Glu, D-Gln, D-His, D-Leu, D-Lys, D-
CC ornithine, D-Trp, D-Val, L-Ala, L-Asp, L-Glu, L-His, L-Leu, L-Lys, L-
CC Met and L-Pro. {ECO:0000269|PubMed:26875494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H2O + O2 = glyoxylate + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:11532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305; EC=1.4.3.19;
CC Evidence={ECO:0000269|PubMed:26875494};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sarcosine = glyoxylate + H2O2 + methylamine;
CC Xref=Rhea:RHEA:15165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:36655, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:59338; EC=1.4.3.19;
CC Evidence={ECO:0000269|PubMed:26875494};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:26875494};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.43 mM for glycine {ECO:0000269|PubMed:26875494};
CC KM=4.86 mM for sarcosine {ECO:0000269|PubMed:26875494};
CC KM=31.7 mM for D-proline {ECO:0000269|PubMed:26875494};
CC KM=7.68 mM for N-ethylglycine {ECO:0000269|PubMed:26875494};
CC Vmax=0.15 umol/min/mg enzyme with glycine as substrate
CC {ECO:0000269|PubMed:26875494};
CC Vmax=0.17 umol/min/mg enzyme with sarcosine as substrate
CC {ECO:0000269|PubMed:26875494};
CC Vmax=0.13 umol/min/mg enzyme with D-proline as substrate
CC {ECO:0000269|PubMed:26875494};
CC Vmax=0.11 umol/min/mg enzyme with N-ethylglycine as substrate
CC {ECO:0000269|PubMed:26875494};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:26875494};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:26875494};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000305|PubMed:26875494}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26875494}.
CC -!- SIMILARITY: Belongs to the DAO family. ThiO subfamily. {ECO:0000305}.
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DR EMBL; AE015451; AAN66238.1; -; Genomic_DNA.
DR RefSeq; NP_742774.1; NC_002947.4.
DR RefSeq; WP_010951878.1; NC_002947.4.
DR AlphaFoldDB; Q88Q83; -.
DR SMR; Q88Q83; -.
DR STRING; 160488.PP_0612; -.
DR EnsemblBacteria; AAN66238; AAN66238; PP_0612.
DR KEGG; ppu:PP_0612; -.
DR PATRIC; fig|160488.4.peg.652; -.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_4_5_6; -.
DR OMA; YPQDAQV; -.
DR PhylomeDB; Q88Q83; -.
DR BioCyc; PPUT160488:G1G01-669-MON; -.
DR BRENDA; 1.4.3.19; 5092.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0043799; F:glycine oxidase activity; IDA:UniProtKB.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009228; P:thiamine biosynthetic process; NAS:UniProtKB.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012727; Gly_oxidase_ThiO.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02352; thiamin_ThiO; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Thiamine biosynthesis.
FT CHAIN 1..365
FT /note="Glycine oxidase"
FT /id="PRO_0000439958"
FT BINDING 12..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O31616"
FT BINDING 32..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O31616"
FT BINDING 40..41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O31616"
FT BINDING 45..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O31616"
FT BINDING 173
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O31616"
FT BINDING 302
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O31616"
FT BINDING 327..333
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O31616"
SQ SEQUENCE 365 AA; 38679 MW; EC0EC9C3A78B6B56 CRC64;
MSKQVVVVGG GVIGLLTAFN LAAKVGQVVV CDQGEVGRES SWAGGGIVSP LYPWRYSPAV
TALAHWSQDF YPQLGERLFA STGVDPEVHT TGLYWLDLDD EAEALAWAAR EQRPLSAVDI
SAAYDAVPVL GPGFKHAIYM AGVANVRNPR LVKSLKAALL ALPNVSLREH CQITGFVQEK
GRVTGVQTAD GVLAADEVVL SAGAWSGDLL RTLGLELPVE PVKGQMILFK CAEDFLPSMV
LAKGRYAIPR RDGHILVGST LEHAGYDKTP TADALESLKA SAVELLPELE GATVVAHWAG
LRPGSPEGIP YIGPVPGHEG LWLNCGHYRN GLVLAPASCQ LFTDLLTGAE PIIDPAPYAP
EGRLG
