THI4_METIK
ID THI4_METIK Reviewed; 263 AA.
AC F6BCS4;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Thiamine thiazole synthase {ECO:0000303|PubMed:26919468};
DE EC=2.4.2.59 {ECO:0000269|PubMed:26919468};
GN Name=thi4 {ECO:0000303|PubMed:26919468};
GN OrderedLocusNames=Metig_0735 {ECO:0000312|EMBL:AEF96285.1};
OS Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanotorris.
OX NCBI_TaxID=880724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5666 / JCM 11834 / Kol 5;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M.,
RA Whitman W., Woyke T.;
RT "Complete sequence of Methanotorris igneus Kol 5.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IRON AND A GLYCINE
RP IMINE INTERMEDIATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
RP PATHWAY.
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:0000255|HAMAP-Rule:MF_00304, ECO:0000305|PubMed:26919468}.
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};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:26919468};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:26919468};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000305|PubMed:26919468}.
CC -!- SUBUNIT: Homooctamer; tetramer of dimers.
CC {ECO:0000269|PubMed:26919468}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_00304}.
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DR EMBL; CP002737; AEF96285.1; -; Genomic_DNA.
DR RefSeq; WP_013798888.1; NC_015562.1.
DR PDB; 4Y4N; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-263.
DR PDBsum; 4Y4N; -.
DR AlphaFoldDB; F6BCS4; -.
DR SMR; F6BCS4; -.
DR STRING; 880724.Metig_0735; -.
DR EnsemblBacteria; AEF96285; AEF96285; Metig_0735.
DR GeneID; 10643575; -.
DR KEGG; mig:Metig_0735; -.
DR HOGENOM; CLU_053727_2_0_2; -.
DR OMA; MWGGGMM; -.
DR OrthoDB; 61905at2157; -.
DR BRENDA; 2.4.2.59; 13534.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000009227; 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 1: Evidence at protein level;
KW 3D-structure; Iron; Metal-binding; NAD; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..263
FT /note="Thiamine thiazole synthase"
FT /id="PRO_0000438857"
FT BINDING 40
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 59..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:0000305|PubMed:26919468"
FT BINDING 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 133
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 159..161
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 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000269|PubMed:26919468"
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:0000269|PubMed:26919468"
FT BINDING 179
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 226
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 236
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000305|PubMed:26919468"
FT HELIX 9..27
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:4Y4N"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 55..64
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4Y4N"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4Y4N"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:4Y4N"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 126..139
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 203..213
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:4Y4N"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:4Y4N"
FT HELIX 242..260
FT /evidence="ECO:0007829|PDB:4Y4N"
SQ SEQUENCE 263 AA; 28128 MW; 282EFB2FC7035ED1 CRC64;
MDVRLRADEY ATTRAILKSA FDMWLDIIDV DVAIVGGGPS GLTAARYIAK EGYKVVVLER
HLAFGGGTWG GGMGFPYIVV EEPADEILRE VGVKLEKVEG EDGLYTADSV EVPAKLAVGA
IDAGAKVLTG IVVEDLVLRE NRVAGVVINS YAIEKAGLHI DPITITAKYV VDATGHDASV
VTTLSRKNPE LGLEVPGEKS MWAEKGENAL LRNTREVYPG LFVCGMAANA VYAGHRMGAI
FGGMYISGKK CAEMIVEKLK NNE
