ID A0A0Q9YRQ7_9COXI Unreviewed; 265 AA.
AC A0A0Q9YRQ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=puo {ECO:0000313|EMBL:KRG18616.1};
GN Synonyms=thi4 {ECO:0000256|HAMAP-Rule:MF_00304};
GN ORFNames=CC99x_01503 {ECO:0000313|EMBL:KRG18616.1};
OS Candidatus Berkiella cookevillensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG18616.1, ECO:0000313|Proteomes:UP000051494};
RN [1] {ECO:0000313|EMBL:KRG18616.1, ECO:0000313|Proteomes:UP000051494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC99 {ECO:0000313|EMBL:KRG18616.1,
RC ECO:0000313|Proteomes:UP000051494};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRG18616.1}.
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DR EMBL; LKHV01000006; KRG18616.1; -; Genomic_DNA.
DR RefSeq; WP_057624596.1; NZ_LKHV02000001.1.
DR AlphaFoldDB; A0A0Q9YRQ7; -.
DR STRING; 437022.CC99x_01503; -.
DR PATRIC; fig|1590042.3.peg.1527; -.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000051494; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 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 Oxidoreductase {ECO:0000313|EMBL:KRG18616.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051494};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00304}; Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT BINDING 39
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 58..59
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 66
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 130
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 161
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 161
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 176
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 223
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 233
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
SQ SEQUENCE 265 AA; 28738 MW; C8A852E14A49955D CRC64;
MMFTQIDEKE ITRAIIHEYH AQLDSAVESD VIIAGAGPSG LVAGRYLAQR GYKVTIIERN
NYLGGGMWIG GYLMNKVTLR APAQAILDEL NIAYKEYKPG LFVADSAFFA SGLIRGACEA
GVTFLNMTIV EDVVVKNKVL TGLVINSMPV TQLPRMITCL DPIIIESKLV IDATGHDAII
CRLLGKRQML ESKGMGPLWV EASEKEIVAR TGEVFPNLII SGMAVSEKCG LPRMGPTFGG
MLLSGKRAGE IACTALETKQ RETTK
//
