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Database: UniProt
Entry: THI4_METMJ
LinkDB: THI4_METMJ
Original site: THI4_METMJ 
ID   THI4_METMJ              Reviewed;         254 AA.
AC   A3CXS4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-JUL-2019, entry version 75.
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=Memar_2251;
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S.,
RA   Hauser L., Land M., Lucas S., Richardson P., Whitman W.B.,
RA   Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al.
RT   1981 type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(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; CP000562; ABN58174.1; -; Genomic_DNA.
DR   RefSeq; WP_011845083.1; NC_009051.1.
DR   SMR; A3CXS4; -.
DR   STRING; 368407.Memar_2251; -.
DR   EnsemblBacteria; ABN58174; ABN58174; Memar_2251.
DR   GeneID; 4846229; -.
DR   KEGG; mem:Memar_2251; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; MMAR368407:G1G85-2259-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000002146; 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    254       Thiamine thiazole synthase.
FT                                /FTId=PRO_0000300738.
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. {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     219    219       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00304}.
FT   BINDING     229    229       Glycine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00304}.
SQ   SEQUENCE   254 AA;  26950 MW;  70DDE680D7D782B9 CRC64;
     MTLNEVTISR AILEEQHRAL IDHLEMDAAV IGGGPSGLAC AALLGEKGVK CALIEKKLSI
     GGGMWGGGMM FPRIVVQEDA RRLLDRFGIA YKAFEEGYYV AKSVEAVAKL TAAACDAGVE
     FFNLTTVEDV MIRGDGRIGG LVVNWTPVDM AGLHVDPLTM ACTCTVDATG HDAMIARMVE
     KKGGALTVKG ESFMWAERAE SQILAHTKEV FPGLFVTGMA ANAVAGECRM GPIFGGMLLS
     GERAAELVAE RLGR
//
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