ID   THIOG_TRIV2             Reviewed;         652 AA.
AC   Q3M859;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=Ava_3219;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA22827.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M859; -.
DR   SMR; Q3M859; -.
DR   STRING; 240292.Ava_3219; -.
DR   PRIDE; Q3M859; -.
DR   EnsemblBacteria; ABA22827; ABA22827; Ava_3219.
DR   KEGG; ava:Ava_3219; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG2022; Bacteria.
DR   HOGENOM; CLU_024913_0_0_3; -.
DR   OMA; QTKAPGH; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000002533; 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   Schiff base; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..652
FT                   /note="Bifunctional protein ThiO/ThiG"
FT                   /id="PRO_0000236329"
FT   REGION          1..366
FT                   /note="ThiO"
FT   REGION          393..652
FT                   /note="ThiG"
FT   ACT_SITE        494
FT                   /note="Schiff-base intermediate with DXP"
FT                   /evidence="ECO:0000250"
FT   BINDING         5..19
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..46
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         301
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000250"
FT   BINDING         325..331
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000250"
FT   BINDING         555
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250"
FT   BINDING         581..582
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250"
FT   BINDING         603..604
FT                   /ligand="1-deoxy-D-xylulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57792"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   652 AA;  70273 MW;  CC632A583086D3A7 CRC64;
     MTRDIVIIGG GVIGLAIAVE LKLRGTKVTV LCRDFPAAAA HAAAGMLAPD AEEITDEAMK
     SLCWRSRSLY PEWTSKLEDL TGLNTGYWPC GILAPVYEGQ ESKGVRIQEN KGESPAYWLE
     KAVIHQYQPG LGEDVVGGWW YPEDAQVNNQ ALARVLWAAA ESLGVELNDG ITVEGLLQQQ
     GQVVGVQTNT GIIQAEHYVL ATGAWANELL PLPVTPRKGQ MLRVRVPESV PELPLKRVLF
     GENIYIVPRR DRSIIIGATS EDVGFTPHNT PAGIQTLLQG AIRLYPQLQD YPIQEFWWGF
     RPATPDELPI LGTSHCANLT LATGHYRNGI LLAPITAALI ADFIVEQKSD PLLSHFHYSR
     FQKQASTTPM FTHSANFSNG HAKNPPLPTL DSSLIIAGKS FHSRLMTGTG KYRSIEEMQQ
     SVVASGCEIV TVAVRRVQTK APGHEGLAEA LDWSRIWMLP NTAGCQTAEE AIRVARLGRE
     MAKLLGQEDN NFVKLEVIPD PKYLLPDPIG TLQAAEQLVK EGFAVLPYIN ADPMLAKRLE
     DVGCATVMPL ASPIGSGQGL KTTANIQIII ENAKIPVVVD AGIGAPSEAS QAMELGADAL
     LINSAIALAQ NPAAMAQAMN LATVAGRLAY LAGRMPIKTY ASASSPVTGT IS