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Database: UniProt
Entry: G0EFR7_PYRF1
LinkDB: G0EFR7_PYRF1
Original site: G0EFR7_PYRF1 
ID   G0EFR7_PYRF1            Unreviewed;       274 AA.
AC   G0EFR7;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   03-JUL-2019, entry version 48.
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=Pyrfu_0366 {ECO:0000313|EMBL:AEM38238.1};
OS   Pyrolobus fumarii (strain DSM 11204 / 1A).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Pyrodictiaceae; Pyrolobus.
OX   NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM38238.1, ECO:0000313|Proteomes:UP000001037};
RN   [1] {ECO:0000313|EMBL:AEM38238.1, ECO:0000313|Proteomes:UP000001037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037};
RX   PubMed=21886865;
RA   Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M.,
RA   Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M.,
RA   Huber H., Yasawong M., Rohde M., Spring S., Abt B., Sikorski J.,
RA   Wirth R., Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of the hyperthermophilic chemolithoautotroph
RT   Pyrolobus fumarii type strain (1A).";
RL   Stand. Genomic Sci. 4:381-392(2011).
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; CP002838; AEM38238.1; -; Genomic_DNA.
DR   STRING; 694429.Pyrfu_0366; -.
DR   EnsemblBacteria; AEM38238; AEM38238; Pyrfu_0366.
DR   KEGG; pfm:Pyrfu_0366; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001037; 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:UP000001037};
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:UP000001037};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      68     69       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     171    173       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       173    173       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       188    188       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      49     49       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      76     76       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     238    238       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     248    248       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   274 AA;  28800 MW;  D0A2B408C665F8DD CRC64;
     MVIPGHMTTR RTAMPGLDAI ITRVIIEEAS KELVEYAESD VIVVGAGPAG LTAAFYLAKR
     GFRVLVLERR LSVGGGIGGG GMLFHKVLVQ EEALPVLNDM GIRVHPTSVK GIYSLDSVAL
     ITGLASAAVN AGAKIILGLE AVDLVVRKEG ERHRVAGVMA LWSAVGIANL HVDPLMFEAK
     AVVDATGHDA RLARIAHQKL RGEAPEVPGD GPAWAEEGEK LVVKATGELI PGLYVAGMAA
     TAVKGYYRMG PIFGGMLLSG KKVADLITEK LRGK
//
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