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Database: UniProt
Entry: S7UT70_9DELT
LinkDB: S7UT70_9DELT
Original site: S7UT70_9DELT 
ID   S7UT70_9DELT            Unreviewed;       263 AA.
AC   S7UT70;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   03-JUL-2019, entry version 23.
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=dsat_2219 {ECO:0000313|EMBL:EPR35518.1};
OS   Desulfovibrio alkalitolerans DSM 16529.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=1121439 {ECO:0000313|EMBL:EPR35518.1, ECO:0000313|Proteomes:UP000014975};
RN   [1] {ECO:0000313|EMBL:EPR35518.1, ECO:0000313|Proteomes:UP000014975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16529 {ECO:0000313|EMBL:EPR35518.1,
RC   ECO:0000313|Proteomes:UP000014975};
RX   PubMed=23950126;
RA   Brown S.D., Hurt R.A.Jr., Gilmour C.C., Elias D.A.;
RT   "Draft genome sequences for three mercury-methylating, sulfate-
RT   reducing bacteria.";
RL   Genome Announc. 1:e00618-13(2013).
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:EPR35518.1}.
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DR   EMBL; ATHI01000004; EPR35518.1; -; Genomic_DNA.
DR   RefSeq; WP_020886105.1; NZ_ATHI01000004.1.
DR   STRING; 1121439.dsat_2219; -.
DR   EnsemblBacteria; EPR35518; EPR35518; dsat_2219.
DR   PATRIC; fig|1121439.3.peg.609; -.
DR   OrthoDB; 1025532at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000014975; 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:UP000014975};
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:UP000014975};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      54     55       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     156    158       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       158    158       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       173    173       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      35     35       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      62     62       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     126    126       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     227    227       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     237    237       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   263 AA;  28150 MW;  21F5EF25BB82E790 CRC64;
     MLDETLVTKA IATRFFEKFL DCVELDVAIV GAGPSGLTCA WKLAEQGFKV AMFERKLSLG
     GGIWGGGMTW NEIVVQEASR HVLDEAGVPL REFAPDHYTA DAVAVTVTLA SKACLAGARI
     FNCMSVEDVC LRGEGDDVRV TGIVINSSPV EIAGLHVDPV AMSCKVLVEA TGHDMEVLRT
     LTRKNGVRLN TPTGQIMGER SMWAEVAEQT TPLNTREVFP GVWVAGMAAN ACYGGYRMGP
     VFGGMLLSGE KAARDIAARL RGE
//
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