GenomeNet

Database: UniProt
Entry: A0A0P9GCJ2_9ARCH
LinkDB: A0A0P9GCJ2_9ARCH
Original site: A0A0P9GCJ2_9ARCH 
ID   A0A0P9GCJ2_9ARCH        Unreviewed;       275 AA.
AC   A0A0P9GCJ2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   03-JUL-2019, entry version 18.
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=AOA66_0043 {ECO:0000313|EMBL:KPV64611.1};
OS   Candidatus Bathyarchaeota archaeon BA2.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1700836 {ECO:0000313|EMBL:KPV64611.1, ECO:0000313|Proteomes:UP000050284};
RN   [1] {ECO:0000313|EMBL:KPV64611.1, ECO:0000313|Proteomes:UP000050284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BA2 {ECO:0000313|EMBL:KPV64611.1};
RX   PubMed=26494757; DOI=10.1126/science.aac7745;
RA   Evans P.N., Parks D.H., Chadwick G.L., Robbins S.J., Orphan V.J.,
RA   Golding S.D., Tyson G.W.;
RT   "Methane metabolism in the archaeal phylum Bathyarchaeota revealed by
RT   genome-centric metagenomics.";
RL   Science 350:434-438(2015).
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:KPV64611.1}.
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; LIHK01000002; KPV64611.1; -; Genomic_DNA.
DR   EnsemblBacteria; KPV64611; KPV64611; AOA66_0043.
DR   KEGG; barb:AOA66_0043; -.
DR   PATRIC; fig|1700836.3.peg.140; -.
DR   KO; K22699; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000050284; 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:UP000050284};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Isomerase {ECO:0000313|EMBL:KPV64611.1};
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      61     62       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND     161    163       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       163    163       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       178    178       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      42     42       NAD; via amide nitrogen.
FT                                {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     133    133       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     228    228       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     238    238       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   275 AA;  28928 MW;  ACDD874F0FBBCFD9 CRC64;
     MMATKIREVE EEAITRAIIR KAMEDWINFA ENDVLIAGAG PAGLTAAMYL AKAGLKTVVF
     ERKLSFGGGI GGGGMQLHKL VVRSPADKIL KEVGCALEKL EDGVYIVDTS AMMAKLAAGA
     IDAGAKIILG VVVEDLIYRG SPPQITGAVV QWTSVIMSGI HVDPLGVKAK AVIDCTGHDA
     EVLAVASRKI PELDIVVPGE KSMWASHAEQ LTVENTKEVC PGLFVAGMAV AALCQTPRMG
     PIFGGMLLSG AKVAHLVARK LLGEKVSPKV IPWPI
//
DBGET integrated database retrieval system