GenomeNet

Database: UniProt
Entry: A0A0K2G8T3_NITMO
LinkDB: A0A0K2G8T3_NITMO
Original site: A0A0K2G8T3_NITMO 
ID   A0A0K2G8T3_NITMO        Unreviewed;       266 AA.
AC   A0A0K2G8T3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   03-JUL-2019, entry version 18.
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=NITMOv2_0947 {ECO:0000313|EMBL:ALA57381.1};
OS   Nitrospira moscoviensis.
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
OX   NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA57381.1, ECO:0000313|Proteomes:UP000069205};
RN   [1] {ECO:0000313|EMBL:ALA57381.1, ECO:0000313|Proteomes:UP000069205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA57381.1,
RC   ECO:0000313|Proteomes:UP000069205};
RX   PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA   Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA   Nielsen P.H., Wagner M., Daims H.;
RT   "Expanded metabolic versatility of ubiquitous nitrite-oxidizing
RT   bacteria from the genus Nitrospira.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP011801; ALA57381.1; -; Genomic_DNA.
DR   RefSeq; WP_053378725.1; NZ_CP011801.1.
DR   EnsemblBacteria; ALA57381; ALA57381; NITMOv2_0947.
DR   KEGG; nmv:NITMOv2_0947; -.
DR   PATRIC; fig|42253.5.peg.929; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 1025532at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000069205; Chromosome.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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:UP000069205};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Isomerase {ECO:0000313|EMBL:ALA57381.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069205};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      61     62       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       167    167       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       182    182       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      42     42       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      69     69       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     135    135       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     167    167       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     230    230       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     240    240       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   266 AA;  28856 MW;  0C5AB4B1EA482B69 CRC64;
     MAKPKPAPLR ERDITRQIAR EYYKEFDQLI ESDVIIVGAG PSGLICAHDL AKMGFRTLIV
     EQSLALGGGF WHGGYLMNKA TICEPANEIL EEIGVPCKKI KDCDGMYMVD PPHATGALVA
     AAYRGGAKVL NLTRVVDLIL RRDGVLEGVV VNNTTAEMAG HDIIHVDPIA LESKIVVDAT
     GHDAVVVELL HKRNLYKPVP GNGAMWVSRS EEEVMDRTGE VYPNCFVIGL AVAAVHGTPR
     MGPAFGSMLL SGRYGAELIK KKLKNE
//
DBGET integrated database retrieval system