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Database: UniProt
Entry: THI4_METBU
LinkDB: THI4_METBU
Original site: THI4_METBU 
ID   THI4_METBU              Reviewed;         258 AA.
AC   Q12U93;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-JUL-2019, entry version 79.
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=Mbur_2109;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z.,
RA   Ting L., Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J.,
RA   Ivanova N., Dalin E., Martinez M., Lapidus A., Hauser L., Land M.,
RA   Thomas T., Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
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; CP000300; ABE52983.1; -; Genomic_DNA.
DR   RefSeq; WP_011500122.1; NC_007955.1.
DR   SMR; Q12U93; -.
DR   EnsemblBacteria; ABE52983; ABE52983; Mbur_2109.
DR   GeneID; 3998191; -.
DR   KEGG; mbu:Mbur_2109; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; MBUR259564:G1G6A-2207-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001979; 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; Reference proteome;
KW   Thiamine biosynthesis; Transferase.
FT   CHAIN         1    258       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000259380.
FT   NP_BIND      55     56       NAD. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   NP_BIND     154    156       NAD; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       156    156       Iron; shared with adjacent protomer.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   METAL       171    171       Iron. {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      36     36       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING      63     63       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     127    127       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
FT   BINDING     224    224       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     234    234       Glycine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
SQ   SEQUENCE   258 AA;  27527 MW;  2A22BE6F609CDBBF CRC64;
     MKLDEVTISR AIIEEFSKVF LDYTDVDVAL VGGGPANLVA AKYLAEAGLK TVIYEKKLAV
     GGGMWAGGMM FPRIVVQEDA LHILDEFGIS YHEYENGYYV ANSIESVGKL ISGATSAGAE
     IFNLVNVEDV MIRENDEICG LVINWTAVEI GKLHVDPLAI RSKVVVDGTG HPAVVCSTVQ
     RKVPGAKLGE LGVVGEKPMW ADVGEKMLLD TTKEVYPNLY VAGMAANAVA GAPRMGPVFG
     GMLLSGKQVA ELIIERLG
//
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