GLYOX_PSEAE
ID GLYOX_PSEAE Reviewed; 364 AA.
AC P33642; Q51527; Q9HVN1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Glycine oxidase {ECO:0000250|UniProtKB:Q88Q83};
DE Short=GO {ECO:0000250|UniProtKB:Q88Q83};
DE EC=1.4.3.19 {ECO:0000250|UniProtKB:Q88Q83};
GN Name=thiO {ECO:0000250|UniProtKB:Q88Q83}; OrderedLocusNames=PA4548;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8682785; DOI=10.1128/jb.178.13.3809-3817.1996;
RA Alm R.A., Mattick J.S.;
RT "Identification of two genes with prepilin-like leader sequences involved
RT in type 4 fimbrial biogenesis in Pseudomonas aeruginosa.";
RL J. Bacteriol. 178:3809-3817(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 193-364.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8097014; DOI=10.1111/j.1365-2958.1993.tb01158.x;
RA Hobbs M., Collie E.S.R., Free P.D., Livingston S.P., Mattick J.S.;
RT "PilS and PilR, a two-component transcriptional regulatory system
RT controlling expression of type 4 fimbriae in Pseudomonas aeruginosa.";
RL Mol. Microbiol. 7:669-682(1993).
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.
CC {ECO:0000250|UniProtKB:Q88Q83}.
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:0000250|UniProtKB:Q88Q83};
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:0000250|UniProtKB:Q88Q83};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q88Q83};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000250|UniProtKB:Q88Q83}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q88Q83}.
CC -!- SIMILARITY: Belongs to the DAO family. ThiO subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78142.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L48934; AAB39269.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07936.1; -; Genomic_DNA.
DR EMBL; Z12154; CAA78142.1; ALT_FRAME; Genomic_DNA.
DR PIR; B83078; B83078.
DR RefSeq; NP_253238.1; NC_002516.2.
DR RefSeq; WP_010895678.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; P33642; -.
DR SMR; P33642; -.
DR STRING; 287.DR97_1852; -.
DR PaxDb; P33642; -.
DR PRIDE; P33642; -.
DR DNASU; 878196; -.
DR EnsemblBacteria; AAG07936; AAG07936; PA4548.
DR GeneID; 878196; -.
DR KEGG; pae:PA4548; -.
DR PATRIC; fig|208964.12.peg.4760; -.
DR PseudoCAP; PA4548; -.
DR HOGENOM; CLU_007884_4_5_6; -.
DR InParanoid; P33642; -.
DR OMA; YPQDAQV; -.
DR PhylomeDB; P33642; -.
DR BioCyc; PAER208964:G1FZ6-4641-MON; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0043799; F:glycine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Thiamine biosynthesis.
FT CHAIN 1..364
FT /note="Glycine oxidase"
FT /id="PRO_0000166164"
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"
FT CONFLICT 20
FT /note="E -> K (in Ref. 1; AAB39269)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="L -> I (in Ref. 1; AAB39269)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="S -> N (in Ref. 1; AAB39269)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="R -> P (in Ref. 1; AAB39269)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..282
FT /note="ASA -> VSV (in Ref. 1; AAB39269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39445 MW; 86C82DC62AA7A811 CRC64;
MSERVVVVGA GVIGLLTARE LALAGLRVTL VERGESGREA SWAGGGIVSP LYPWRYSPAV
TALAHWSQDF YPALGQRLLD ETGLDPEVHT VGLYWLDLDD QTEALQWARK HTRPLKEVPI
EEAYAAVPGL GAGFQRAVYM SGVANVRNPR LARSLRASLQ QFANLELHEQ TEVRGWLRDG
DRVVGVATSR GEIRGDKVLL AAGAWSGELL KPLGLELPVV PVKGQMILYK CAADFLPRMV
LAKGRYAIPR RDGHILIGST LEHSGFDKTP TDEAQESLRA SAAELLPELA DMQPVAHWAG
LRPGSPEGIP YIGPVPGFDG LWLNTGHYRN GLVLAPASCR LLADLMSGRE PIIDPAPYAP
AGRL
