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Database: UniProt
Entry: R5GDL8_9BACT
LinkDB: R5GDL8_9BACT
Original site: R5GDL8_9BACT 
ID   R5GDL8_9BACT            Unreviewed;       257 AA.
AC   R5GDL8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   03-JUL-2019, entry version 20.
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=BN773_01414 {ECO:0000313|EMBL:CCY15450.1};
OS   Prevotella sp. CAG:755.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella; environmental samples.
OX   NCBI_TaxID=1262935 {ECO:0000313|EMBL:CCY15450.1, ECO:0000313|Proteomes:UP000018353};
RN   [1] {ECO:0000313|EMBL:CCY15450.1, ECO:0000313|Proteomes:UP000018353}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:755 {ECO:0000313|Proteomes:UP000018353};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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}.
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:CCY15450.1}.
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DR   EMBL; CAXR010000058; CCY15450.1; -; Genomic_DNA.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000018353; 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:UP000018353};
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:UP000018353};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     151    153       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       153    153       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       168    168       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      34     34       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      61     61       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     125    125       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     222    222       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     232    232       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   257 AA;  27456 MW;  F4C9BA5824097755 CRC64;
     MIEIQVSEGI ISTYFEKMRR CLDLDVAIVG GGPSGIVAAY YLAKAGLRVA QFDRKLSPGG
     GMWGGAMMFN QIVIQEEALP IVKDFGISYA PYKDGLYTMD SVESTSALLY QAVHAGATVF
     NCYSVEDVVY KDNRVSGVVV NWTPVLREGL HVDPLNIMAR CVIDGTGHDS EICRTVARKN
     GARLATETGD VVGERSLDVA TGEEEVVCGT KEIYPGLYVC GMAASAVSGT PRMGPIFGGM
     LLSGKKVADL IIAKLKA
//
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