THIOG_SYNY3
ID THIOG_SYNY3 Reviewed; 656 AA.
AC Q55710; Q55064;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Bifunctional protein ThiO/ThiG;
DE Includes:
DE RecName: Full=Probable FAD-dependent glycine oxidase;
DE EC=1.4.3.19;
DE Includes:
DE RecName: Full=Thiazole synthase;
DE EC=2.8.1.10;
GN Name=thiO/thiG; OrderedLocusNames=slr0633;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bulteau S., Cassier-Chauvat C., Chauvat F.;
RT "Cloning, expression and inactivation of the ruvB gene from the
RT cyanobacterium Synechocystis PCC6803.";
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the FAD-dependent oxidative deamination of glycine.
CC Is essential for thiamine biosynthesis since the oxidation of glycine
CC catalyzed by ThiO generates the glycine imine intermediate
CC (dehydroglycine) required for the biosynthesis of the thiazole ring of
CC thiamine pyrophosphate. {ECO:0000250}.
CC -!- FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate
CC (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is
CC provided by the thiocarboxylate moiety of the carrier protein ThiS. In
CC vitro, sulfur can be provided by H(2)S. {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + [sulfur-
CC carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH = 2-[(2R,5Z)-2-
CC carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-
CC carrier protein ThiS]-C-terminal Gly-Gly + 2 H(+) + 2 H2O;
CC Xref=Rhea:RHEA:26297, Rhea:RHEA-COMP:12908, Rhea:RHEA-COMP:12909,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:62899, ChEBI:CHEBI:77846, ChEBI:CHEBI:90619,
CC ChEBI:CHEBI:90778; EC=2.8.1.10;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBUNIT: Interacts with ThiH and ThiS. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DAO family. ThiO
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiG family.
CC {ECO:0000305}.
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DR EMBL; U38892; AAA96395.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10351.1; -; Genomic_DNA.
DR PIR; S76505; S76505.
DR AlphaFoldDB; Q55710; -.
DR SMR; Q55710; -.
DR IntAct; Q55710; 3.
DR STRING; 1148.1001620; -.
DR PaxDb; Q55710; -.
DR EnsemblBacteria; BAA10351; BAA10351; BAA10351.
DR KEGG; syn:slr0633; -.
DR eggNOG; COG0665; Bacteria.
DR eggNOG; COG2022; Bacteria.
DR InParanoid; Q55710; -.
DR OMA; QTKAPGH; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:1990107; F:thiazole synthase activity; IEA:RHEA.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04728; ThiG; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00443; ThiG; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012727; Gly_oxidase_ThiO.
DR InterPro; IPR033983; Thiazole_synthase_ThiG.
DR InterPro; IPR008867; ThiG.
DR PANTHER; PTHR34266; PTHR34266; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF05690; ThiG; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02352; thiamin_ThiO; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Multifunctional enzyme; Oxidoreductase;
KW Reference proteome; Schiff base; Thiamine biosynthesis; Transferase.
FT CHAIN 1..656
FT /note="Bifunctional protein ThiO/ThiG"
FT /id="PRO_0000162867"
FT REGION 1..395
FT /note="ThiO"
FT REGION 396..656
FT /note="ThiG"
FT ACT_SITE 498
FT /note="Schiff-base intermediate with DXP"
FT /evidence="ECO:0000250"
FT BINDING 7..21
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 48..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250"
FT BINDING 322..328
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 324
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000250"
FT BINDING 585..586
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000250"
FT BINDING 607..608
FT /ligand="1-deoxy-D-xylulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:57792"
FT /evidence="ECO:0000250"
FT CONFLICT 454
FT /note="A -> R (in Ref. 1; AAA96395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 70271 MW; 93FAD1A915A0FA23 CRC64;
MQTTSDVLII GGGIIGLAIA VELKLKQKRL QVTVLSRDFA QAASHAAAGM LAPHAEQIAP
GPMLDLCLAS RWRYGEWVEK LEQLTGMETG YNPCGILSPV FEAPHGNSST NSAWLDQETI
RYYQPGLGED VIGGWWHPDD GQVDNRKLVS ALRQAAQSLG VQIQEGVTVQ AIAQRHGQVT
AVLTDQGSFQ ADSYVLANGS WAKELLPLPV FPVKGQMMAL RMPAGTHQPY PLQRVLFGPQ
TYLVPRRDGR LIVGATSEQV DWQPHNTPQG IQTLLGRAIR LFPALGDWAI EDFWWGFRPG
TPDEQPFLGY GPCDNLILAI GHYRNGILLA PITAALISDL ILDQKVSPLI HAFSPQRFLT
TTNPPVLSCR PMTAVFPSIA NPSLPHAAEN SEGSKDLLEI AGRKFHSRLM TGTGKYPSLT
TMQESVASSG CQIVTVAVRR VQTNAPGHEG LAEAIDWSTI WMLPNTAGCQ TAEEAIRVAR
LGREMAKLLG QEDNNFIKLE VIPDTQYLLP DPIGTLEAAE QLVKEGFAVL PYINADPLLA
KRLEEVGCAT VMPLGSPIGS GQGIRNAANI GIIIENAKVP VVVDAGIGTP SEAAQAMEMG
ADAVLINSAI AMAANPVAMA QAMGMATQAG RLAYLSGRMP IKAKANASSP LTGLVG
