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Database: UniProt
Entry: D3I0T1_9BACT
LinkDB: D3I0T1_9BACT
Original site: D3I0T1_9BACT 
ID   D3I0T1_9BACT            Unreviewed;       259 AA.
AC   D3I0T1;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Thiamine thiazole synthase {ECO:0000256|HAMAP-Rule:MF_00304};
DE            EC=2.4.2.59 {ECO:0000256|HAMAP-Rule:MF_00304};
GN   Name=thi4 {ECO:0000256|HAMAP-Rule:MF_00304};
GN   ORFNames=HMPREF0649_02113 {ECO:0000313|EMBL:EFC74913.1};
OS   Prevotella buccae D17.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575611 {ECO:0000313|EMBL:EFC74913.1, ECO:0000313|Proteomes:UP000005080};
RN   [1] {ECO:0000313|EMBL:EFC74913.1, ECO:0000313|Proteomes:UP000005080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D17 {ECO:0000313|EMBL:EFC74913.1,
RC   ECO:0000313|Proteomes:UP000005080};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Sibley C.D., White A., Allen-Vercoe E., Strauss J., Crowley S.,
RA   Surette M.G., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella buccae Oral Taxon 560 strain D17.";
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of the thiazole moiety of
CC       thiamine. Catalyzes the conversion of NAD and glycine to adenosine
CC       diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an
CC       adenylated thiazole intermediate, using free sulfide as a source of
CC       sulfur. {ECO:0000256|HAMAP-Rule:MF_00304}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine + hydrogen sulfide + NAD(+) = ADP-5-ethyl-4-
CC         methylthiazole-2-carboxylate + H(+) + 3 H2O + nicotinamide;
CC         Xref=Rhea:RHEA:55704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29919, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:139151; EC=2.4.2.59;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00304};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00304};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00304}.
CC   -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC       Rule:MF_00304}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC       Rule:MF_00304}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00304}.
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DR   EMBL; GG739950; EFC74913.1; -; Genomic_DNA.
DR   RefSeq; WP_004343049.1; NZ_GG739950.1.
DR   AlphaFoldDB; D3I0T1; -.
DR   HOGENOM; CLU_053727_2_0_10; -.
DR   OrthoDB; 9777740at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000005080; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016763; F:pentosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   HAMAP; MF_00304; Thi4; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR002922; Thi4_fam.
DR   InterPro; IPR022828; Thi4_prok.
DR   NCBIfam; TIGR00292; sulfide-dependent adenosine diphosphate thiazole synthase; 1.
DR   PANTHER; PTHR43422; THIAMINE THIAZOLE SYNTHASE; 1.
DR   PANTHER; PTHR43422:SF3; THIAMINE THIAZOLE SYNTHASE; 1.
DR   Pfam; PF01946; Thi4; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00304};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00304}; NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00304}; Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent protomers"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT   BINDING         61
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent protomers"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT   BINDING         125
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent protomers"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT   BINDING         151..153
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent protomers"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT   BINDING         153
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared between two adjacent protomers"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="ligand shared between two adjacent protomers"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT   BINDING         222
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /ligand_note="ligand shared between two adjacent protomers"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT   BINDING         232
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
SQ   SEQUENCE   259 AA;  28030 MW;  5D2A722CDEFB4626 CRC64;
     MIEKQVSRGI IRTYFEKLDR NLELDVAIVG GGPSGIVAAY YMAKAGLRVA LFDRKLSPGG
     GMWGGAMMFN QIVVQREALG IIEDFGIRYE PYEDELFTVD SIESTSALLY KAVHEGATLF
     NCYSVEDVVF KDNAVSGVVV NWTPVLREGL HVDPLNIMAR FVVDGTGHDS EMCRVVARKN
     GISLATATGE VVGERSLDVV EGERLVVEGT KEIYPGLYVC GMASSAVSGT PRMGPIFGGM
     LLSGKKVADD IIARIKGRL
//
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