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Database: UniProt
Entry: W0JPR0_9EURY
LinkDB: W0JPR0_9EURY
Original site: W0JPR0_9EURY 
ID   W0JPR0_9EURY            Unreviewed;       309 AA.
AC   W0JPR0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   03-JUL-2019, entry version 25.
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=HALLA_10200 {ECO:0000313|EMBL:AHF99164.1};
OS   Halostagnicola larsenii XH-48.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Natrialbales; Natrialbaceae; Halostagnicola.
OX   NCBI_TaxID=797299 {ECO:0000313|EMBL:AHF99164.1, ECO:0000313|Proteomes:UP000019024};
RN   [1] {ECO:0000313|EMBL:AHF99164.1, ECO:0000313|Proteomes:UP000019024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XH-48 {ECO:0000313|EMBL:AHF99164.1,
RC   ECO:0000313|Proteomes:UP000019024};
RG   DOE Joint Genome Institute;
RA   Anderson I., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N.,
RA   Schaumberg A., Pati A., Liolios K., Nordberg H.P., Cantor M.N.,
RA   Hua S.X., Woyke T.;
RL   Submitted (JAN-2014) 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; CP007055; AHF99164.1; -; Genomic_DNA.
DR   RefSeq; WP_049952372.1; NZ_CP007055.1.
DR   STRING; 797299.HALLA_10200; -.
DR   EnsemblBacteria; AHF99164; AHF99164; HALLA_10200.
DR   GeneID; 25144833; -.
DR   KEGG; hlr:HALLA_10200; -.
DR   PATRIC; fig|797299.3.peg.1069; -.
DR   KO; K22699; -.
DR   OrthoDB; 61905at2157; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000019024; 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:UP000019024};
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:UP000019024};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      62     63       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       168    168       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       183    183       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      43     43       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      70     70       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     168    168       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     258    258       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     268    268       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   309 AA;  32948 MW;  071B88BA6A91499C CRC64;
     MSEFEKFSDV GEADVTRAIG QEWTEEFMDF SDSDVIIVGG GPSGLTAAKE LSERGVKVMV
     VEKNNYLGGG FWLGGFLMNK VTVRSPAQKV LDELDVSYKE SQDSEDLYVA NGPEACSGLI
     KAACDAGAKM QNMTEFTDIV IRENHRVGGI VMNWTPVHAL PREITCVDPI AVEADLVIDA
     TGHDAMAVTK LDERGVLDAP GIQDAKERGQ VMDQTDSDTY GAPGHDSPGH DSMWVGESED
     AVVEHTGLVH DGLIATGMAT ATTFGLPRMG PTFGAMLVSG KRAAQVALDE LEVEADPVEL
     TSRAAPADD
//
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