ID   THIOG_NOSS1             Reviewed;         652 AA.
AC   Q8YRC9;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=all3519;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000019; BAB75218.1; -; Genomic_DNA.
DR   PIR; AH2245; AH2245.
DR   RefSeq; WP_010997669.1; NZ_RSCN01000015.1.
DR   AlphaFoldDB; Q8YRC9; -.
DR   SMR; Q8YRC9; -.
DR   STRING; 103690.17132652; -.
DR   EnsemblBacteria; BAB75218; BAB75218; BAB75218.
DR   KEGG; ana:all3519; -.
DR   eggNOG; COG0665; Bacteria.
DR   eggNOG; COG2022; Bacteria.
DR   OMA; QTKAPGH; -.
DR   OrthoDB; 784095at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000002483; 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..652
FT                   /note="Bifunctional protein ThiO/ThiG"
FT                   /id="PRO_0000162776"
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;  70114 MW;  3AB2FFF7B1B35130 CRC64;
     MTRDIVIIGG GVIGLAIAVE LKLRGAEVTV ICRDFQAAAA HAAAGMLAPD AEQITDGAMK
     SLCWRSRSLY SEWTSKLEDL TGLNTGYWPC GILAPIYEGQ ESKGVRVQEG EGESPAYWLE
     KAAIHQYQPG LGEDVVGGWW YPEDAQVNNQ ALARVLWAAA ESLGVELKDG ITVEGLLQQQ
     GQVVGVQTNT GIIRAEHYVL ATGAWANELL PLPVTPRKGQ MLRLRVPESV PELPLKRVLF
     GKNIYIVPRR ERSIIVGATS EDVGFTPHNT PAGIQTLLQG AIRLYPQLQD YPIQEFWWGF
     RPATPDELPI LGTSHCPNLT LATGHYRNGI LLAPITAALI ADLIVEQKSD PLLSHFHYSR
     SQKQASTIPM LTHSANFSNG HTKNPPLPTL DSPLIIAGKS FHSRLMTGTG KYRSIEEMQQ
     SVVASGCEIV TVAVRRVQTK TPGHEGLAEA LDWSKIWMLP NTAGCQTAEE AIRVARLGRE
     MAKLLGQEDN NFVKLEVIPD PKYLLPDPIG TLQAAEQLVK EGFAVLPYIN ADPMLAKHLE
     DVGCATVMPL ASPIGSGQGL KTTANIQIII ENAKIPVVVD AGIGAPSEAS QAMELGADAL
     LINSAIALAQ NPAAMAQAMN LATVAGRLAY LAGRMPMKTY ASASSPVTGT IS