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Database: UniProt
Entry: THI4_HALWD
LinkDB: THI4_HALWD
Original site: THI4_HALWD 
ID   THI4_HALWD              Reviewed;         307 AA.
AC   Q18KP1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-JUL-2019, entry version 80.
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};
GN   OrderedLocusNames=HQ_1276A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(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
CC       (ADT), an adenylated thiazole intermediate, using free sulfide as
CC       a source of 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}.
DR   EMBL; AM180088; CAJ51405.1; -; Genomic_DNA.
DR   RefSeq; WP_011570564.1; NC_008212.1.
DR   SMR; Q18KP1; -.
DR   STRING; 362976.HQ_1276A; -.
DR   EnsemblBacteria; CAJ51405; CAJ51405; HQ_1276A.
DR   GeneID; 4192223; -.
DR   KEGG; hwa:HQ_1276A; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; GIVMNWT; -.
DR   OrthoDB; 61905at2157; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001975; Chromosome.
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; IPR022828; Thi4_prok.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Iron; Metal-binding; NAD; Reference proteome;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN         1    307       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000259379.
FT   NP_BIND      61     62       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       167    167       Iron; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       182    182       Iron. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      42     42       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      69     69       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     167    167       NAD; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     257    257       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     267    267       Glycine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
SQ   SEQUENCE   307 AA;  32487 MW;  5C160E7824F7330E CRC64;
     MSFDEFADVS EAQVTRAIAK DWGNEFIDRV DTEVIIVGGG PSGLVTAKEL AERGVDVTIV
     EKNNYLGGGF WLGGFLMNKV TVRDPAQSVL DELDVPYEES DEASGLYVAD GPHAVSSLIK
     SACDAGAEVQ NMTEFTDVVT RENHRVGGIV LNWTPVHALP RELTCVDPVA VESDLVVDST
     GHDAVVISKL SERGVLNAPG IEHANEHNTG MDNTADDEYG APGHDSPGHD SMWVSRSEDQ
     VVEHTGVVHP GVVATGMAVA TVEGLPRMGP TFGAMLLSGK RGAQACLNEL GREATPIDFT
     PAAPADD
//
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