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Database: UniProt
Entry: M0CAL8_9EURY
LinkDB: M0CAL8_9EURY
Original site: M0CAL8_9EURY 
ID   M0CAL8_9EURY            Unreviewed;       310 AA.
AC   M0CAL8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   03-JUL-2019, entry version 30.
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=C475_20967 {ECO:0000313|EMBL:ELZ20285.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales; Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ20285.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ20285.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ20285.1,
RC   ECO:0000313|Proteomes:UP000011626};
RX   PubMed=25393412;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
RA   Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea
RT   reveals strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ELZ20285.1}.
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DR   EMBL; AOIU01000047; ELZ20285.1; -; Genomic_DNA.
DR   RefSeq; WP_006885856.1; NZ_AOIU01000047.1.
DR   STRING; 797114.C475_20967; -.
DR   EnsemblBacteria; ELZ20285; ELZ20285; C475_20967.
DR   PATRIC; fig|797114.5.peg.4227; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; HCAR797114:G1HEU-4175-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000011626; Unassembled WGS sequence.
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:UP000011626};
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:UP000011626};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      64     65       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   REGION      201    228       Disordered. {ECO:0000256|MobiDB-lite:
FT                                M0CAL8}.
FT   METAL       170    170       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       185    185       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      45     45       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      72     72       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     170    170       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     257    257       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     267    267       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   310 AA;  32855 MW;  CBB7B69262ED5374 CRC64;
     MSQEGFDKFS DVGEAEVTRA IGQEWTEEFM DFSDSDVIIV GGGPSGLMAA KELAERGVQV
     MVVEKNNYLG GGFWLGGFLM NKVTVRDPAQ QVLDELDVDH KQSKDSEGLY VANGPEACSG
     LIKAACDAGA KMQNMTEFTD IVIREDHRVG GIVMNWTPVH ALPREITCVD PIAVEADLVI
     DATGHDAMAV KKLDERGVLN APGIGEENSG MDQTGDDTYG APGHDSPGHD SMWVGESEDA
     VVEHTGLAHD GLVVTGMATA TTYGLPRMGP TFGAMLVSGK RAAQVALDEL EVDADPVDLT
     SRDAVASADD
//
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