GenomeNet

Database: UniProt
Entry: B5ID81_ACIB4
LinkDB: B5ID81_ACIB4
Original site: B5ID81_ACIB4 
ID   B5ID81_ACIB4            Unreviewed;       254 AA.
AC   B5ID81;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   03-JUL-2019, entry version 78.
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=Aboo_0963 {ECO:0000313|EMBL:ADD08772.1};
GN   ORFNames=ABOONEI_1525 {ECO:0000313|EMBL:EDY35740.1};
OS   Aciduliprofundum boonei (strain DSM 19572 / T469).
OC   Archaea; Euryarchaeota; Diaforarchaea group; DHVE2 group;
OC   Aciduliprofundum.
OX   NCBI_TaxID=439481 {ECO:0000313|Proteomes:UP000094021};
RN   [1] {ECO:0000313|EMBL:EDY35740.1, ECO:0000313|Proteomes:UP000094021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000094021}, and T469
RC   {ECO:0000313|EMBL:EDY35740.1};
RX   PubMed=18445019; DOI=10.1111/j.1472-4669.2008.00152.x;
RA   Reysenbach A.L., Flores G.E.;
RT   "Electron microscopy encounters with unusual thermophiles helps direct
RT   genomic analysis of Aciduliprofundum boonei.";
RL   Geobiology 6:331-336(2008).
RN   [2] {ECO:0000313|EMBL:ADD08772.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=T469 {ECO:0000313|EMBL:ADD08772.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L.,
RA   Woyke T.;
RT   "Complete sequence of Aciduliprofundum boonei T469.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19572 / T469 {ECO:0000313|Proteomes:UP000001400};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Saunders E., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Flores G., Reysenbach A.-L.,
RA   Woyke T.;
RT   "Complete sequence of Aciduliprofundum boonei T469.";
RL   Submitted (FEB-2010) 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001941; ADD08772.1; -; Genomic_DNA.
DR   EMBL; DS990520; EDY35740.1; -; Genomic_DNA.
DR   RefSeq; WP_008084257.1; NZ_DS990520.1.
DR   STRING; 439481.Aboo_0963; -.
DR   EnsemblBacteria; ADD08772; ADD08772; Aboo_0963.
DR   EnsemblBacteria; EDY35740; EDY35740; ABOONEI_1525.
DR   GeneID; 8827917; -.
DR   KEGG; abi:Aboo_0963; -.
DR   eggNOG; arCOG00574; Archaea.
DR   eggNOG; COG1635; LUCA.
DR   HOGENOM; HOG000106048; -.
DR   KO; K22699; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 61905at2157; -.
DR   BioCyc; ABOO439481:G1GHM-977-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001400; Chromosome.
DR   Proteomes; UP000094021; 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:UP000001400,
KW   ECO:0000313|Proteomes:UP000094021};
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:UP000001400};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       151    151       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       166    166       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      35     35       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      62     62       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     151    151       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     220    220       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     230    230       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   254 AA;  27672 MW;  196E89D93E2EE3CC CRC64;
     MLDEVEITKL IVENYMKDLM EYADLDVAIV GAGPSGLTAA YYLATAKKKV AIFDRRLSIG
     GGMWGGGMMF NKIVVQEDAK HILDDFSINY ERFGDYYVAD SVHSVTSLAY HATKEGAKIF
     NLIGAEDVII KNNRVSGLVI NWSVIGELPI DPLSIYAKYV IDATGHESEV IKTLVRKNNI
     KLNTPTGSIE GEHSMDADTA ESVIVDNVKE VYPGIFVTGM AANAVFGSPR MGPIFGGMLL
     SGKKVADEII RRLS
//
DBGET integrated database retrieval system