THI4_METJA
ID THI4_METJA Reviewed; 267 AA.
AC Q58018;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thiamine thiazole synthase {ECO:0000303|PubMed:26928142};
DE EC=2.4.2.59 {ECO:0000269|PubMed:26919468, ECO:0000269|PubMed:26928142};
GN Name=thi4 {ECO:0000303|PubMed:26928142}; OrderedLocusNames=MJ0601;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND PRELIMINARY FUNCTION IN CO(2) FIXATION
RP WITH RUBISCO.
RX PubMed=15375115; DOI=10.1128/jb.186.19.6360-6366.2004;
RA Finn M.W., Tabita F.R.;
RT "Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic
RT archaea.";
RL J. Bacteriol. 186:6360-6366(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, AND REACTION MECHANISM.
RX PubMed=26928142; DOI=10.1021/jacs.6b00445;
RA Eser B.E., Zhang X., Chanani P.K., Begley T.P., Ealick S.E.;
RT "From suicide enzyme to catalyst: The iron-dependent sulfide transfer in
RT Methanococcus jannaschii thiamin thiazole biosynthesis.";
RL J. Am. Chem. Soc. 138:3639-3642(2016).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH ADP-RIBULOSE,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, REACTION MECHANISM,
RP MUTAGENESIS OF HIS-164, AND LACK OF RUBP SYNTHASE ACTIVITY.
RX PubMed=26919468; DOI=10.1021/acs.biochem.6b00030;
RA Zhang X., Eser B.E., Chanani P.K., Begley T.P., Ealick S.E.;
RT "Structural basis for iron-mediated sulfur transfer in archael and yeast
RT thiazole synthases.";
RL Biochemistry 55:1826-1838(2016).
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:0000269|PubMed:26919468, ECO:0000269|PubMed:26928142}.
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:0000269|PubMed:26919468, ECO:0000269|PubMed:26928142};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:26919468, ECO:0000269|PubMed:26928142};
CC Note=Binds 1 Fe(2+) ion per subunit. Other divalent metal cations can
CC support activity. {ECO:0000269|PubMed:26928142};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000305|PubMed:26928142}.
CC -!- SUBUNIT: Homooctamer; tetramer of dimers.
CC {ECO:0000269|PubMed:26919468}.
CC -!- MISCELLANEOUS: Unlike THI4 from S.cerevisiae, Thi4 from M.jannaschii
CC can catalyze multiple turnovers because the sulfide is not enzyme
CC derived. {ECO:0000305|PubMed:26928142}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000305}.
CC -!- CAUTION: This protein was originally thought to have NAD-dependent
CC ribose 1,5-bisphosphate isomerase activity but the recombinant protein
CC was not active in vitro (PubMed:15375115, PubMed:26919468). In
CC contrast, another protein from M.jannaschii likely possesses this
CC activity (MJ0122). {ECO:0000305|PubMed:15375115,
CC ECO:0000305|PubMed:26919468}.
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DR EMBL; L77117; AAB98592.1; -; Genomic_DNA.
DR PIR; A64375; A64375.
DR PDB; 4Y4M; X-ray; 2.71 A; A/B/C/D/E/F/G/H=1-267.
DR PDBsum; 4Y4M; -.
DR AlphaFoldDB; Q58018; -.
DR SMR; Q58018; -.
DR STRING; 243232.MJ_0601; -.
DR EnsemblBacteria; AAB98592; AAB98592; MJ_0601.
DR KEGG; mja:MJ_0601; -.
DR eggNOG; arCOG00574; Archaea.
DR HOGENOM; CLU_053727_2_0_2; -.
DR InParanoid; Q58018; -.
DR PhylomeDB; Q58018; -.
DR BioCyc; MetaCyc:MON-21800; -.
DR BRENDA; 2.4.2.59; 3260.
DR BRENDA; 2.4.2.60; 3260.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Iron; Metal-binding; NAD;
KW Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..267
FT /note="Thiamine thiazole synthase"
FT /id="PRO_0000153947"
FT BINDING 47
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:0000305|PubMed:26919468"
FT BINDING 66..67
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:0000305|PubMed:26919468"
FT BINDING 74
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:0000305|PubMed:26919468"
FT BINDING 138
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:0000305|PubMed:26919468"
FT BINDING 164..166
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000305|PubMed:26919468"
FT BINDING 166
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 181
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 184
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:0000305|PubMed:26919468"
FT BINDING 230
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:0000305|PubMed:26919468"
FT BINDING 240
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT MUTAGEN 164
FT /note="H->C: Still requires free sulfide for ADT synthesis,
FT showing that this cysteine cannot act as an enzyme-derived
FT sulfur source for thiazole formation as in S.cerevisiae."
FT /evidence="ECO:0000269|PubMed:26919468"
FT HELIX 16..34
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 46..57
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:4Y4M"
FT TURN 74..78
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4Y4M"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:4Y4M"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 131..144
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:4Y4M"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:4Y4M"
FT HELIX 246..263
FT /evidence="ECO:0007829|PDB:4Y4M"
SQ SEQUENCE 267 AA; 28655 MW; 2F359B900C838251 CRC64;
MVNLMNIKDI KLNADETKTT KAILKASFDM WLDIVEADVV IVGAGPSGLT CARYLAKEGF
KVVVLERHLA FGGGTWGGGM GFPYIVVEEP ADELLREVGI KLIDMGDGYY VADSVEVPAK
LAVAAMDAGA KILTGIVVED LILREDGVAG VVINSYAIER AGLHIDPLTI RSKVVVDATG
HEASIVNILV KKNKLEADVP GEKSMWAEKG ENALLRNTRE VYPNLFVCGM AANASHGGYR
MGAIFGGMYL SGKLCAELIT EKLKNKE
