THI4_PYRAE
ID THI4_PYRAE Reviewed; 261 AA.
AC Q8ZZM5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00304};
DE EC=2.4.2.59 {ECO:0000255|HAMAP-Rule:MF_00304};
GN Name=thi4 {ECO:0000255|HAMAP-Rule:MF_00304}; OrderedLocusNames=PAE0175;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_00304};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00304};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00304}.
CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00304}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_00304}.
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DR EMBL; AE009441; AAL62614.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZZM5; -.
DR SMR; Q8ZZM5; -.
DR STRING; 178306.PAE0175; -.
DR EnsemblBacteria; AAL62614; AAL62614; PAE0175.
DR KEGG; pai:PAE0175; -.
DR PATRIC; fig|178306.9.peg.126; -.
DR eggNOG; arCOG00574; Archaea.
DR HOGENOM; CLU_053727_2_0_2; -.
DR InParanoid; Q8ZZM5; -.
DR OMA; MWGGGMM; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002439; 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; -; 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 SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00292; TIGR00292; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; NAD; Reference proteome; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..261
FT /note="Thiamine thiazole synthase"
FT /id="PRO_1000115613"
FT BINDING 33
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:0000255|HAMAP-Rule:MF_00304"
FT BINDING 52..53
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:0000255|HAMAP-Rule:MF_00304"
FT BINDING 60
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:0000255|HAMAP-Rule:MF_00304"
FT BINDING 124
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:0000255|HAMAP-Rule:MF_00304"
FT BINDING 152..154
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 169
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:0000255|HAMAP-Rule:MF_00304"
FT BINDING 219
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:0000255|HAMAP-Rule:MF_00304"
FT BINDING 229
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
SQ SEQUENCE 261 AA; 27721 MW; 2A25AB7AAD7FB6ED CRC64;
MELKIGRAII SHALKDLDEY SDVDVAIVGA GPAGLTAARY LAEKGLKVVV YERRFSFGGG
IGPGGNMLPK IVVQEEAVPI LRDFKVRYKP AEDGLYTVDP AELIAKLAAG AVDAGAKIIL
GVHVDDVIFR GDPPRVTGLL WIWTPIQMSG MHVDPLYTQA KAVIDATGHD AEVVSVAARK
VPELGIQVVG EKSAWSEVSE KLVVEHTGRV APGLYVAGIA VCAVYGLPRM GPIFGGMLMS
GKKVAEVVYK DLMAEAHAVR A
