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Database: UniProt
Entry: F7PLY7_9EURY
LinkDB: F7PLY7_9EURY
Original site: F7PLY7_9EURY 
ID   F7PLY7_9EURY            Unreviewed;       307 AA.
AC   F7PLY7;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-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   ORFNames=HLRTI_001608 {ECO:0000313|EMBL:ERJ06403.1}, HTIA_2465
GN   {ECO:0000313|EMBL:CCQ34573.1};
OS   Halorhabdus tiamatea SARL4B.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales; Haloarculaceae; Halorhabdus.
OX   NCBI_TaxID=1033806 {ECO:0000313|EMBL:ERJ06403.1, ECO:0000313|Proteomes:UP000003861};
RN   [1] {ECO:0000313|EMBL:ERJ06403.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06403.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=21705593; DOI=10.1128/JB.05462-11;
RA   Antunes A., Alam I., Bajic V.B., Stingl U.;
RT   "Genome sequence of Halorhabdus tiamatea, the first archaeon isolated
RT   from a deep-sea anoxic brine lake.";
RL   J. Bacteriol. 193:4553-4554(2011).
RN   [2] {ECO:0000313|EMBL:ERJ06403.1, ECO:0000313|Proteomes:UP000003861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|EMBL:ERJ06403.1,
RC   ECO:0000313|Proteomes:UP000003861};
RX   PubMed=24324765;
RA   Alam I., Antunes A., Kamau A.A., Ba Alawi W., Kalkatawi M., Stingl U.,
RA   Bajic V.B.;
RT   "INDIGO - INtegrated Data Warehouse of MIcrobial GenOmes with Examples
RT   from the Red Sea Extremophiles.";
RL   PLoS ONE 8:E82210-E82210(2013).
RN   [3] {ECO:0000313|EMBL:CCQ34573.1, ECO:0000313|Proteomes:UP000015381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381}, and Type strain:
RC   SARL4B {ECO:0000313|EMBL:CCQ34573.1};
RX   PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA   Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA   Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M.,
RA   Antunes A., Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O.,
RA   Golyshina O.V., Golyshin P.N., Teeling H.;
RT   "Halorhabdus tiamatea: proteogenomics and glycosidase activity
RT   measurements identify the first cultivated euryarchaeon from a deep-
RT   sea anoxic brine lake as potential polysaccharide degrader.";
RL   Environ. Microbiol. 16:2525-2537(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; HF571520; CCQ34573.1; -; Genomic_DNA.
DR   EMBL; AFNT02000016; ERJ06403.1; -; Genomic_DNA.
DR   RefSeq; WP_008527083.1; NZ_AFNT02000016.1.
DR   STRING; 1033806.HTIA_2465; -.
DR   EnsemblBacteria; CCQ34573; CCQ34573; HTIA_2465.
DR   EnsemblBacteria; ERJ06403; ERJ06403; HLRTI_001608.
DR   GeneID; 23798993; -.
DR   KEGG; hti:HTIA_2465; -.
DR   PATRIC; fig|1033806.12.peg.2453; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   KO; K22699; -.
DR   OrthoDB; 61905at2157; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000003861; Unassembled WGS sequence.
DR   Proteomes; UP000015381; 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:UP000003861,
KW   ECO:0000313|Proteomes:UP000015381};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Isomerase {ECO:0000313|EMBL:ERJ06403.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015381};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      64     65       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   REGION      203    227       Disordered. {ECO:0000256|MobiDB-lite:
FT                                F7PLY7}.
FT   METAL       170    170       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       185    185       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      45     45       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      72     72       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     170    170       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     257    257       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     267    267       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   307 AA;  32712 MW;  EE37928B3BC0A6F5 CRC64;
     MHANEFDQFS DVGEATVTRA ITQEWTDEFM DFTESDVIII GGGPSGLMAA KELTERGVKT
     MVVEKNNYLG GGFWLGGFLM NKVTVRDPAQ YVLDELDVEY TQSEEDDGLY VANGPEATSG
     LIKATCDAGA KMQNMTEFTD IVVREDHRVG GIVMNWTPVH ALPREITCVD PIAVESDLVI
     DATGHEALAI KKLDERGVLD AEGIEEGATG MDATDEESYG APGHDSPGHD SMWVAESEDA
     VVEHTGLVHD GLIATGMAVA TAHGLPRMGP TFGAMLLSGK RGAQVALDEL GVDADPVDMT
     TPAPADD
//
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