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Database: UniProt
Entry: A0A1G9SXN9_9EURY
LinkDB: A0A1G9SXN9_9EURY
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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
//
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