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Database: UniProt
Entry: A0A285P0U7_9EURY
LinkDB: A0A285P0U7_9EURY
Original site: A0A285P0U7_9EURY 
ID   A0A285P0U7_9EURY        Unreviewed;       307 AA.
AC   A0A285P0U7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   03-JUL-2019, entry version 7.
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=SAMN06269185_2237 {ECO:0000313|EMBL:SNZ13501.1};
OS   Natronoarchaeum philippinense.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Halobacteriales; Halobacteriaceae.
OX   NCBI_TaxID=558529 {ECO:0000313|EMBL:SNZ13501.1, ECO:0000313|Proteomes:UP000219453};
RN   [1] {ECO:0000313|EMBL:SNZ13501.1, ECO:0000313|Proteomes:UP000219453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27208 {ECO:0000313|EMBL:SNZ13501.1,
RC   ECO:0000313|Proteomes:UP000219453};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; OBEJ01000002; SNZ13501.1; -; Genomic_DNA.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000219453; 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:UP000219453};
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:UP000219453};
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    219       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A285P0U7}.
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     255    255       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     265    265       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   307 AA;  32592 MW;  612B6CE24BAF3ABC CRC64;
     MSEFDQFSDV GEAEVTRAIG QEWSEEFMDF SETEVIIVGG GPSGLMAAKE LSERGVQTMV
     VEKNNYLGGG FWLGGFLMNK VTVRDPAQQV LDELAVDYKQ SEESDGLYVA NGPEACSGLI
     KAACDAGAKM QNMTEFTDIV IREDHRVGGI VMNWTPVHAL PREITCVDPI AVEADLVIDA
     TGHDGMAVKK LDERGVLDAP GFEEEASGMD STDDDTYGAP GHDSPGHDSM WVGESEDAVV
     EHTGLAHEGL VVTGMATATT YGLPRMGPTF GAMLVSGKRA AQVALDELGV DADPVDETAS
     KATPADD
//
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