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THI4_METBF
ID   THI4_METBF              Reviewed;         260 AA.
AC   Q46AR1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=Mbar_A2100;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ71031.1; -; Genomic_DNA.
DR   RefSeq; WP_011307077.1; NC_007355.1.
DR   AlphaFoldDB; Q46AR1; -.
DR   SMR; Q46AR1; -.
DR   STRING; 269797.Mbar_A2100; -.
DR   EnsemblBacteria; AAZ71031; AAZ71031; Mbar_A2100.
DR   GeneID; 3625715; -.
DR   KEGG; mba:Mbar_A2100; -.
DR   eggNOG; arCOG00574; Archaea.
DR   HOGENOM; CLU_053727_2_0_2; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   UniPathway; UPA00060; -.
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; Thiamine biosynthesis; Transferase.
FT   CHAIN           1..260
FT                   /note="Thiamine thiazole synthase"
FT                   /id="PRO_0000259381"
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00304"
FT   BINDING         154..156
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         156
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         171
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         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:0000255|HAMAP-Rule:MF_00304"
FT   BINDING         234
FT                   /ligand="glycine"
FT                   /ligand_id="ChEBI:CHEBI:57305"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
SQ   SEQUENCE   260 AA;  28086 MW;  3ECC522EA6383924 CRC64;
     MELDEVIITR AIFDEYSKTF LDYTEVDVAL IGGGPANLVA ARYLAEAGAK VAIYEQKLSL
     GGGMWAGGMM FPRIVVQEEA CRILDDFGIR YKEYQPGYYV ANSVESVGKL ISGATSAGAE
     VFNLVSFEDV MIRENDRVTG IVVNWGPVTV QRLHVDPLMI RTKLVIDGTG HEAVVCNTIL
     RKIPNAKIGN LGKLGEKPMW SEVGEQLVVD ATKEIYPGLI VAGMAANAAT CSPRMGPVFG
     GMLLSGEKAA KLALEKLKEL
 
 
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