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Database: UniProt
Entry: L0JMY6_NATP1
LinkDB: L0JMY6_NATP1
Original site: L0JMY6_NATP1 
ID   L0JMY6_NATP1            Unreviewed;       309 AA.
AC   L0JMY6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, 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=Natpe_2830 {ECO:0000313|EMBL:AGB32629.1};
GN   ORFNames=C488_13208 {ECO:0000313|EMBL:ELY73762.1};
OS   Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 /
OS   NCIMB 786 / 157).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Natrialbales; Natrialbaceae; Natrinema.
OX   NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB32629.1, ECO:0000313|Proteomes:UP000010843};
RN   [1] {ECO:0000313|Proteomes:UP000010843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC   {ECO:0000313|Proteomes:UP000010843};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGB32629.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 15624 {ECO:0000313|EMBL:AGB32629.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000011593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 {ECO:0000313|Proteomes:UP000011593};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
RA   Darling A., Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ELY73762.1, ECO:0000313|Proteomes:UP000011593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15624 {ECO:0000313|EMBL:ELY73762.1,
RC   ECO:0000313|Proteomes:UP000011593};
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}.
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DR   EMBL; CP003372; AGB32629.1; -; Genomic_DNA.
DR   EMBL; AOIE01000076; ELY73762.1; -; Genomic_DNA.
DR   RefSeq; WP_006182009.1; NZ_AOIE01000076.1.
DR   STRING; 797303.Natpe_2830; -.
DR   EnsemblBacteria; AGB32629; AGB32629; Natpe_2830.
DR   EnsemblBacteria; ELY73762; ELY73762; C488_13208.
DR   GeneID; 14333410; -.
DR   KEGG; npe:Natpe_2830; -.
DR   PATRIC; fig|797303.5.peg.2665; -.
DR   KO; K22699; -.
DR   OMA; GIVMNWT; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; NPEL797303:G1H0T-2731-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000010843; Chromosome.
DR   Proteomes; UP000011593; 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:UP000010843,
KW   ECO:0000313|Proteomes:UP000011593};
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:UP000010843};
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   REGION      199    234       Disordered. {ECO:0000256|MobiDB-lite:
FT                                L0JMY6}.
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   309 AA;  32622 MW;  9FF2F155F599F44E CRC64;
     MSEFEQFSQV GEADVTRAIG QEWTEEFMDF SDSDVIIVGG GPSGLTAAKE LSERGVQTMV
     VEKNNYLGGG FWLGGFLMNK VTVRDPAQEI LADLDVDFKE SQDSEGLYVA NGPEACSGLI
     KAACDAGAKM QNMTEFTDIV IREDHRVGGI VMNWTPVHAL PREITCVDPI AVEADLVIDA
     TGHDAMAVKK LDERGVLDAP GIGDAEASAT GMDQTGDDSY GAPGHDSPGH DSMWVGKSED
     AVVEHTGLVH DGLIATGMAT ATTYGLPRMG PTFGAMLVSG KRAAQEALDE LGVDADPVEL
     TSRATPADD
//
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