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Database: UniProt
Entry: THI4_PYRHO
LinkDB: THI4_PYRHO
Original site: THI4_PYRHO 
ID   THI4_PYRHO              Reviewed;         252 AA.
AC   O59082;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-JUL-2019, entry version 126.
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=PH1357;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 /
OS   NBRC 100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
RA   Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
RA   Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
RA   Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA30463.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BA000001; BAA30463.1; ALT_INIT; Genomic_DNA.
DR   PIR; G71007; G71007.
DR   RefSeq; WP_048053375.1; NC_000961.1.
DR   SMR; O59082; -.
DR   STRING; 70601.3257780; -.
DR   EnsemblBacteria; BAA30463; BAA30463; BAA30463.
DR   GeneID; 1443683; -.
DR   KEGG; pho:PH1357; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; PHOR70601:G1G39-1324-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000752; 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; 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; Iron; Metal-binding; NAD; Thiamine biosynthesis;
KW   Transferase.
FT   CHAIN         1    252       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000153953.
FT   NP_BIND      54     55       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   NP_BIND     152    154       NAD; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       154    154       Iron; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       169    169       Iron. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      35     35       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      62     62       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     126    126       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     217    217       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     227    227       Glycine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
SQ   SEQUENCE   252 AA;  27245 MW;  C92A58226CDBA4C5 CRC64;
     MLREVTITRA IVESYYRDLL NNLELDVAIV GAGPSGMVAA YYLAKGGAKV AIFEKKLSIG
     GGIWGGGMGF NKVVVQDEAR EILDEFGIRY EEFEKGYYVA DAIEVATTIA SKVVKSGVKI
     FNMIEVEDLV IKDNRVSGIV INWTPVLMAG LHVDPLTIEA KYVIDSTGHG AQVAQFLVKR
     GLLKEIPGEG AMWAEQGEKL TVKNTREVFP GLYVTGMAAN AIAGAPRMGP IFGGMFLSGR
     KAAQEILKKL KS
//
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