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Database: UniProt
Entry: M0CXG4_9EURY
LinkDB: M0CXG4_9EURY
Original site: M0CXG4_9EURY 
ID   M0CXG4_9EURY            Unreviewed;       308 AA.
AC   M0CXG4;
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=C474_17304 {ECO:0000313|EMBL:ELZ27127.1};
OS   Halogeometricum pallidum JCM 14848.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Halogeometricum.
OX   NCBI_TaxID=1227487 {ECO:0000313|EMBL:ELZ27127.1, ECO:0000313|Proteomes:UP000011513};
RN   [1] {ECO:0000313|EMBL:ELZ27127.1, ECO:0000313|Proteomes:UP000011513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14848 {ECO:0000313|EMBL:ELZ27127.1,
RC   ECO:0000313|Proteomes:UP000011513};
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:ELZ27127.1}.
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DR   EMBL; AOIV01000041; ELZ27127.1; -; Genomic_DNA.
DR   RefSeq; WP_008389021.1; NZ_AOIV01000041.1.
DR   STRING; 1227487.C474_17304; -.
DR   EnsemblBacteria; ELZ27127; ELZ27127; C474_17304.
DR   PATRIC; fig|1227487.5.peg.3428; -.
DR   OrthoDB; 61905at2157; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000011513; 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:UP000011513};
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:UP000011513};
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   308 AA;  32436 MW;  20EF08E53FB7C638 CRC64;
     MSEFSGFADV SEAQVTRAIA SDWTEEFMDR IDTEVIVVGG GPSGLMAAKE LAKRDVDVAI
     VEKNNYLGGG FWLGGFLMNK VTVRDPAQSV LDELGVPYEE AEEAPGLYVA DGPHACSALI
     EAACDAGANV QNMTEFTDVV VREDHRVGGV VLNWTPVHAL PRELTCVDPV AVESDLVLDA
     TGHDAVVISK LTERGVLDAP GIEHAKEHNT GMDQTEEGEY GAPGHDSPGH DSMWVGESED
     AVVENTGLVH PGVVASGMAV ATVNGLPRMG PTFGAMLISG KRAAQSIMDE LGRDGPEIEF
     SPAAPADD
//
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