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Database: UniProt
Entry: G7WRI7_METH6
LinkDB: G7WRI7_METH6
Original site: G7WRI7_METH6 
ID   G7WRI7_METH6            Unreviewed;       259 AA.
AC   G7WRI7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   03-JUL-2019, entry version 50.
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   OrderedLocusNames=Mhar_2378 {ECO:0000313|EMBL:AET65728.1};
OS   Methanosaeta harundinacea (strain 6Ac).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosaetaceae; Methanothrix.
OX   NCBI_TaxID=1110509 {ECO:0000313|EMBL:AET65728.1, ECO:0000313|Proteomes:UP000005877};
RN   [1] {ECO:0000313|EMBL:AET65728.1, ECO:0000313|Proteomes:UP000005877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6Ac {ECO:0000313|EMBL:AET65728.1,
RC   ECO:0000313|Proteomes:UP000005877};
RX   PubMed=22590603; DOI=10.1371/journal.pone.0036756;
RA   Zhu J., Zheng H., Ai G., Zhang G., Liu D., Liu X., Dong X.;
RT   "The genome characteristics and predicted function of methyl-group
RT   oxidation pathway in the obligate aceticlastic methanogens,
RT   Methanosaeta spp.";
RL   PLoS ONE 7:E36756-E36756(2012).
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; CP003117; AET65728.1; -; Genomic_DNA.
DR   RefSeq; WP_014587904.1; NC_017527.1.
DR   EnsemblBacteria; AET65728; AET65728; Mhar_2378.
DR   GeneID; 12511557; -.
DR   KEGG; mhi:Mhar_2378; -.
DR   PATRIC; fig|1110509.7.peg.2630; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; MHAR1110509:GLGF-2378-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000005877; Chromosome.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:UP000005877};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Isomerase {ECO:0000313|EMBL:AET65728.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005877};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      55     56       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     154    156       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       156    156       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       171    171       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      36     36       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      63     63       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     127    127       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     224    224       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     234    234       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   259 AA;  27429 MW;  490FE1F8F32C2CCE CRC64;
     MALDEVTITK AIVESYMDSF LKYTDVDVAL VGAGPANLVA AKKLAEADAK TVVFERNLAV
     GGGIWGGGMM FPRIVVQKEG CRILDEFGVW YREYAEGYYI ASSIETVAKL TAGVVDAGAE
     IINLVAVEDV MIREDERVAG LVINWEAVER TRLHVDPLSV RAKVVIDGTG HDANICKVVQ
     RKIPGARVGS LGVPGEKPMW ADVGERTVVE VTQEVYPGLI AAGMAATAVA GGPRMGPIFG
     GMLLSGEKAA AIALEKLGL
//
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