THI4_META3
ID THI4_META3 Reviewed; 263 AA.
AC A6UV59;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Maeo_0798;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL Submitted (JUN-2007) 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: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; CP000743; ABR56381.1; -; Genomic_DNA.
DR AlphaFoldDB; A6UV59; -.
DR SMR; A6UV59; -.
DR STRING; 419665.Maeo_0798; -.
DR EnsemblBacteria; ABR56381; ABR56381; Maeo_0798.
DR KEGG; mae:Maeo_0798; -.
DR eggNOG; arCOG00574; Archaea.
DR HOGENOM; CLU_053727_2_0_2; -.
DR OMA; MWGGGMM; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001106; 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..263
FT /note="Thiamine thiazole synthase"
FT /id="PRO_1000196829"
FT BINDING 43
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 62..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 70
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 134
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 160..162
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 162
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 177
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 180
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 227
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 237
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
SQ SEQUENCE 263 AA; 27667 MW; B4855ACD84803BBD CRC64;
MDISKIDLKA DEKAVTKSIF KATYEMWMDN LEVDVVIVGG GPSGLTAGRY LADAGVKVLI
LERHLSFGGG TWGGGMGCPY ITVQSPADEI LSEVGIKLEE GEDGLFVADS VEVPAKLGTG
AIDAGAKVLT GIVVEDVILK EGKVSGVVIN SYAINKAGLH IDPLTINAKY VIDATGHDAS
VACTLARKNE DLGLVIPGEK SLWADEGENG LLKYTKELFP GLFVCGMASN ATHGGYRMGA
VFGGMYISGK IVADMILEKL KNE
