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Database: UniProt
Entry: A0A1H3H862_9EURY
LinkDB: A0A1H3H862_9EURY
Original site: A0A1H3H862_9EURY 
ID   A0A1H3H862_9EURY        Unreviewed;       308 AA.
AC   A0A1H3H862;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   03-JUL-2019, entry version 8.
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=SAMN04487946_106216 {ECO:0000313|EMBL:SDY11540.1};
OS   Halobellus clavatus.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Halobellus.
OX   NCBI_TaxID=660517 {ECO:0000313|EMBL:SDY11540.1, ECO:0000313|Proteomes:UP000199170};
RN   [1] {ECO:0000313|EMBL:SDY11540.1, ECO:0000313|Proteomes:UP000199170}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10118 {ECO:0000313|EMBL:SDY11540.1,
RC   ECO:0000313|Proteomes:UP000199170};
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
CC       (ADT), an adenylated thiazole intermediate, using free sulfide as
CC       a source of 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; Evidence={ECO:0000256|HAMAP-
CC         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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00304}.
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DR   EMBL; FNPB01000006; SDY11540.1; -; Genomic_DNA.
DR   BioCyc; GCF_900107195:BLU74_RS10900-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000199170; Unassembled WGS sequence.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; 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   Complete proteome {ECO:0000313|Proteomes:UP000199170};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199170};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      61     62       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       166    166       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       181    181       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      42     42       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      69     69       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     166    166       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     256    256       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     266    266       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   308 AA;  32248 MW;  5349A34A3E0E5F97 CRC64;
     MSFSGFSHAT DAQVTEAITK SWSDEFLDFT DTEVIVVGGG PSGLVTAKEL AERGVDVMIV
     EKNNYLGGGF WLGGFLMNKL TVREPADTVL DELGVPYEES DTEGLHLADG PHACSSLIAA
     ACDAGARIQN MTEFTDVVVR DDHRVAGIVM NWSPVHALPR ELTCVDPIAV EADLVVDATG
     HDAVVVSKLQ EQGVVDAPGI EHAAAHETGM DTTDDGEYGA PGHDSPGHDS MWAADSEDKV
     VEKTGKIHEG LLTAGLSTAT THGLTRMGPT FGAMLLSGKR AAQVALDELG TNAPTVDLPG
     DTPASADD
//
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