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Database: UniProt
Entry: D4GSS5_HALVD
LinkDB: D4GSS5_HALVD
Original site: D4GSS5_HALVD 
ID   D4GSS5_HALVD            Unreviewed;       307 AA.
AC   D4GSS5; L9UNI3;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   03-JUL-2019, entry version 70.
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   ECO:0000313|EMBL:ADE05087.1};
GN   OrderedLocusNames=HVO_0665 {ECO:0000313|EMBL:ADE05087.1};
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
OS   14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE05087.1, ECO:0000313|Proteomes:UP000008243};
RN   [1] {ECO:0000313|Proteomes:UP000008243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S.,
RA   Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M.,
RA   Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T.,
RA   Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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; CP001956; ADE05087.1; -; Genomic_DNA.
DR   RefSeq; WP_004044270.1; NZ_AOHU01000097.1.
DR   STRING; 309800.C498_15398; -.
DR   EnsemblBacteria; ADE05087; ADE05087; HVO_0665.
DR   EnsemblBacteria; ELY26470; ELY26470; C498_15398.
DR   GeneID; 8924004; -.
DR   KEGG; hvo:HVO_0665; -.
DR   PATRIC; fig|309800.29.peg.2977; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; GIVMNWT; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; HVOL309800:GCOK-668-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000008243; 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:UP000008243};
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:UP000008243};
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     167    167       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;  32424 MW;  5A803FA06801153D CRC64;
     MSFDGFTDAT EAQVTRAISD SWMEEFRERT DTEVIVVGGG PSGLVAAKEL AERGVDVTIV
     EKNNYLGGGF WLGGFLMNKV TVRDPAQRVL DELGVPYEES DEAEGLYVAD GPHACSALIK
     AACDAGAKIQ NMTEFTDVVL REDDRVGGIV MNWTPVHALP RELTCVDPIA VESDLVLDAT
     GHDAVVLSKL SERGVLDVNG IEHAKEHNTG MDKTADGEYG APGHDSPGHD SMWVSESEDS
     IVDATGVVHP GVVASGMAVA TAHHLPRMGP TFGAMLLSGR QAAQSCLDEL GRDAPDVSIS
     GPAPADD
//
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