GenomeNet

Database: UniProt
Entry: A0A151BJ83_9ARCH
LinkDB: A0A151BJ83_9ARCH
Original site: A0A151BJ83_9ARCH 
ID   A0A151BJ83_9ARCH        Unreviewed;       267 AA.
AC   A0A151BJ83;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   03-JUL-2019, entry version 15.
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=AYL32_013970 {ECO:0000313|EMBL:KYH39985.1};
OS   Candidatus Bathyarchaeota archaeon B26-2.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1779371 {ECO:0000313|EMBL:KYH39985.1, ECO:0000313|Proteomes:UP000075437};
RN   [1] {ECO:0000313|EMBL:KYH39985.1, ECO:0000313|Proteomes:UP000075437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B26-2 {ECO:0000313|EMBL:KYH39985.1};
RA   He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S.,
RA   Wang F.;
RT   "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT   phylum Bathyarchaeota widespread in marine sediments.";
RL   Submitted (MAR-2016) 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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KYH39985.1}.
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; LUCE01000048; KYH39985.1; -; Genomic_DNA.
DR   PATRIC; fig|1779371.3.peg.1078; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000075437; Unassembled WGS sequence.
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:UP000075437};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Isomerase {ECO:0000313|EMBL:KYH39985.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      58     59       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     160    162       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       162    162       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       177    177       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      39     39       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      66     66       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     130    130       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     227    227       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     237    237       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   267 AA;  28569 MW;  5CB4E9A414F57024 CRC64;
     MRIKEVDEAV VTKAILEGSL KYLHELTEVD VAVVGAGPAG LTASRYLAKA GLKTVVFERR
     LSFGGGIGGG GMQLPMLVVQ SPADEILREV GCNLTTYREG VYLANSSEML AKLAYSAVKA
     GAHIILGVTV DDLIYRSEEN RTRIVGVVVQ WSSVIISGLH VDPLAFKAGA VVDCTGHDAE
     VLSVASRKIP ELNLMIQGEK AMWVSESERL IVEKTGEVSP GLYVAGMAVA TLNQTPRMGP
     IFGGMLLSGK KVAEIIIERY KQNRTQG
//
DBGET integrated database retrieval system