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Database: UniProt
Entry: H1Z0Q1_9EURY
LinkDB: H1Z0Q1_9EURY
Original site: H1Z0Q1_9EURY 
ID   H1Z0Q1_9EURY            Unreviewed;       265 AA.
AC   H1Z0Q1;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   03-JUL-2019, entry version 29.
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   ORFNames=Metlim_1198 {ECO:0000313|EMBL:EHQ35308.1};
OS   Methanoplanus limicola DSM 2279.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX   NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ35308.1, ECO:0000313|Proteomes:UP000005741};
RN   [1] {ECO:0000313|EMBL:EHQ35308.1, ECO:0000313|Proteomes:UP000005741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ35308.1,
RC   ECO:0000313|Proteomes:UP000005741};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Wirth R.,
RA   Brambilla E.-M., Klenk H.-P., Eisen J.A.;
RT   "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT   2279.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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; CM001436; EHQ35308.1; -; Genomic_DNA.
DR   EnsemblBacteria; EHQ35308; EHQ35308; Metlim_1198.
DR   PATRIC; fig|937775.9.peg.1374; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000005741; 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 {ECO:0000313|Proteomes:UP000005741};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005741};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      66     67       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     165    167       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       167    167       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       182    182       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      47     47       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      74     74       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     138    138       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     230    230       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     240    240       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   265 AA;  28283 MW;  EF4E3235CD00F49B CRC64;
     MKTKVYESEN KMKLDEVAIS RAIVSEQSKV MLDYYDLDCA IVGAGPSGLT CAAMLGEEGL
     KVGVIEKKLS VGGGMWGGGM TFPRIVVQEE ARRLLDHFGI KYREYESGYF VSSSVEAVAK
     ITSAACDAGA EFFNLTYVED VVIKGDNRIS GLVINQTPIQ MTGLHIDPLT LATKVTIDAT
     GHDSVVAHLV RDKGGSVEIK GEGFMWADRA ESNILSHTKE IFPGLIVTGM AANAVGGETR
     MGPVFGGMLL SGEKAAKLAK SALKK
//
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