ID A0A1G9SXN9_9EURY Unreviewed; 311 AA.
AC A0A1G9SXN9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Thiamine thiazole synthase {ECO:0000256|HAMAP-Rule:MF_00304};
DE EC=2.4.2.59 {ECO:0000256|HAMAP-Rule:MF_00304};
GN Name=thi4 {ECO:0000256|HAMAP-Rule:MF_00304};
GN ORFNames=SAMN05192554_10221 {ECO:0000313|EMBL:SDM40190.1};
OS Haloarchaeobius iranensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halorubellaceae; Haloarchaeobius.
OX NCBI_TaxID=996166 {ECO:0000313|EMBL:SDM40190.1, ECO:0000313|Proteomes:UP000199370};
RN [1] {ECO:0000313|EMBL:SDM40190.1, ECO:0000313|Proteomes:UP000199370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB21,IBRC-M 10013,KCTC 4048
RC {ECO:0000313|Proteomes:UP000199370};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|HAMAP-Rule:MF_00304};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00304};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00304}.
CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000256|HAMAP-
CC Rule:MF_00304}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC Rule:MF_00304}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00304}.
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DR EMBL; FNIA01000002; SDM40190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9SXN9; -.
DR STRING; 996166.SAMN05192554_10221; -.
DR OrthoDB; 4240at2157; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000199370; Unassembled WGS sequence.
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; FAD/NAD(P)-binding domain; 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 NCBIfam; TIGR00292; sulfide-dependent adenosine diphosphate thiazole synthase; 1.
DR PANTHER; PTHR43422; THIAMINE THIAZOLE SYNTHASE; 1.
DR PANTHER; PTHR43422:SF3; THIAMINE THIAZOLE SYNTHASE; 1.
DR Pfam; PF01946; Thi4; 2.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00304};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00304}; NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW Reference proteome {ECO:0000313|Proteomes:UP000199370};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00304}; Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00304"
FT BINDING 168
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT BINDING 168
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
FT BINDING 183
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:0000256|HAMAP-Rule:MF_00304"
FT BINDING 258
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:0000256|HAMAP-Rule:MF_00304"
FT BINDING 268
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00304"
SQ SEQUENCE 311 AA; 32817 MW; EE99EC9601B2E7DC CRC64;
MDDFDSFADV GEAEVTRAIG QEWSEEFLDF SDSEVIIVGG GPSGLTAAKE LAERGVKVMV
VEKNNYLGGG FWLGGFLMNK VTVRDPAQGI LDDLDVEYDE AGDVDGLYVA NGPEACSGLI
KAACDAGAKM QNMTEFTDIV VREDHRVSGI VMNYTPVHAL PREITCVDPV AVEADLVIDS
TGHDAMAINK LDERGVLDAP GIQAANERGE VMDQTGDDSY GAPGHDSPGH DSMWVGRSED
EVVEHTGVVH DGLVASGMAV ATAYGLPRMG PTFGAMLVSG KKAAQVALDE LDKDVEPVTL
SDSRAAAPAD D
//