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Database: UniProt
Entry: F2NC70_DESAR
LinkDB: F2NC70_DESAR
Original site: F2NC70_DESAR 
ID   F2NC70_DESAR            Unreviewed;       261 AA.
AC   F2NC70;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   03-JUL-2019, entry version 45.
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   OrderedLocusNames=Desac_0998 {ECO:0000313|EMBL:AEB08865.1};
OS   Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophaceae; Desulfobacca.
OX   NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB08865.1, ECO:0000313|Proteomes:UP000000483};
RN   [1] {ECO:0000313|EMBL:AEB08865.1, ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RX   PubMed=21886866;
RA   Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA   Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of the acetate-degrading sulfate reducer
RT   Desulfobacca acetoxidans type strain (ASRB2).";
RL   Stand. Genomic Sci. 4:393-401(2011).
RN   [2] {ECO:0000313|Proteomes:UP000000483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC   {ECO:0000313|Proteomes:UP000000483};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL   Submitted (MAR-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; CP002629; AEB08865.1; -; Genomic_DNA.
DR   RefSeq; WP_013705978.1; NC_015388.1.
DR   STRING; 880072.Desac_0998; -.
DR   EnsemblBacteria; AEB08865; AEB08865; Desac_0998.
DR   KEGG; dao:Desac_0998; -.
DR   eggNOG; ENOG4105IQJ; Bacteria.
DR   eggNOG; COG1635; LUCA.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 1025532at2; -.
DR   BioCyc; DACE880072:G1GSP-1002-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000483; 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:UP000000483};
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:UP000000483};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      55     56       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     153    155       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       155    155       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       170    170       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      36     36       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      63     63       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     127    127       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     225    225       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     235    235       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   261 AA;  28505 MW;  AC9A7919A58F21A1 CRC64;
     MGLDEIIISR AIIERFMEKF LDNLELDVAI VGGGVSGLVA GWRLAQKGRK AAIFERKLSV
     GGGMWGGGMM FNEIVVQEEA KHLLDELGIT SRPYDRGYYT ADAIESTTTL ASQAMKAGVK
     IFNLIHVEDV MVRENRIDGL VILWTAVNMA GLHVDPLTIR AKHVIDCTGH DVEVIKIFLR
     KNQPASLKTE TGGIMGERSM WAEVGEAKTV EYTSEVYPGL WVAGMTATGT LGTFRMGPIF
     GGMMLSGEKA ANLIDERLKK G
//
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