ID B1I303_DESAP Unreviewed; 259 AA.
AC B1I303;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
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 OrderedLocusNames=Daud_0859 {ECO:0000313|EMBL:ACA59372.1};
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforudis.
OX NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA59372.1, ECO:0000313|Proteomes:UP000008544};
RN [1] {ECO:0000313|Proteomes:UP000008544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACA59372.1, ECO:0000313|Proteomes:UP000008544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C {ECO:0000313|EMBL:ACA59372.1,
RC ECO:0000313|Proteomes:UP000008544};
RX PubMed=18845759; DOI=10.1126/science.1155495;
RA Chivian D., Brodie E.L., Alm E.J., Culley D.E., Dehal P.S., Desantis T.Z.,
RA Gihring T.M., Lapidus A., Lin L.H., Lowry S.R., Moser D.P.,
RA Richardson P.M., Southam G., Wanger G., Pratt L.M., Andersen G.L.,
RA Hazen T.C., Brockman F.J., Arkin A.P., Onstott T.C.;
RT "Environmental genomics reveals a single-species ecosystem deep within
RT Earth.";
RL Science 322:275-278(2008).
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; CP000860; ACA59372.1; -; Genomic_DNA.
DR RefSeq; WP_012301958.1; NC_010424.1.
DR AlphaFoldDB; B1I303; -.
DR STRING; 477974.Daud_0859; -.
DR KEGG; dau:Daud_0859; -.
DR eggNOG; COG1635; Bacteria.
DR HOGENOM; CLU_053727_2_0_9; -.
DR OrthoDB; 9806565at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000008544; Chromosome.
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; PR00420; RNGMNOXGNASE.
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 Reference proteome {ECO:0000313|Proteomes:UP000008544};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00304}; Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT BINDING 36
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 55..56
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 63
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 127
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 153..155
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 155
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 170
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 173
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 224
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 234
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
SQ SEQUENCE 259 AA; 27735 MW; 5FD19217DDB4AE26 CRC64;
MKLDETIISR AIIESYVTRL LSCLEVDVEI VGGGPSGLTA AYYLARAGLK TTVYERKLSV
GGGMWGGAAM MNEIVFQETA RPVFEEFGVT IKKYRDNYYT ASSVECVAAL TLGACRAGAN
IMNLLTVEDV VLHNNRVSGL VLNWSAVEIS GLHVDPIATR SKFVVDATGH DVSVVGVLAR
KAGVQLDTPS GKVQGEKPMW ADLGEAQIME NTSEIFPGLY VVGMAANAVH GGYRMGAVFG
GMVLSGRRVA EMIIDRLKV
//
