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Database: UniProt
Entry: A0A0A7V7T3_9ARCH
LinkDB: A0A0A7V7T3_9ARCH
Original site: A0A0A7V7T3_9ARCH 
ID   A0A0A7V7T3_9ARCH        Unreviewed;       276 AA.
AC   A0A0A7V7T3;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   03-JUL-2019, entry version 24.
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=A7X95_00600 {ECO:0000313|EMBL:PTL87822.1}, T478_0555
GN   {ECO:0000313|EMBL:AJA92730.1};
OS   Candidatus Nitrosopelagicus brevis.
OC   Archaea; Thaumarchaeota; unclassified Thaumarchaeota.
OX   NCBI_TaxID=1410606 {ECO:0000313|EMBL:AJA92730.1, ECO:0000313|Proteomes:UP000030944};
RN   [1] {ECO:0000313|EMBL:AJA92730.1, ECO:0000313|Proteomes:UP000030944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN25 {ECO:0000313|EMBL:AJA92730.1}, and V2
RC   {ECO:0000313|Proteomes:UP000030944};
RX   PubMed=25587132; DOI=10.1073/pnas.1416223112;
RA   Santoro A.E., Dupont C.L., Richter R.A., Craig M.T., Carini P.,
RA   McIlvin M.R., Yang Y., Orsi W.D., Moran D.M., Saito M.A.;
RT   "Genomic and proteomic characterization of "Candidatus
RT   Nitrosopelagicus brevis": an ammonia-oxidizing archaeon from the open
RT   ocean.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:1173-1178(2015).
RN   [2] {ECO:0000313|EMBL:PTL87822.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL87822.1};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|Proteomes:UP000241022};
RA   Dupont C., Santoro A.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:PTL87822.1, ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL87822.1,
RC   ECO:0000313|Proteomes:UP000241022};
RA   Carini P.;
RT   "Transcriptomics of ammonia oxidizing archaea.";
RL   Submitted (APR-2018) 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; CP007026; AJA92730.1; -; Genomic_DNA.
DR   EMBL; LXWN01000001; PTL87822.1; -; Genomic_DNA.
DR   RefSeq; WP_048106821.1; NZ_LXWN01000001.1.
DR   EnsemblBacteria; AJA92730; AJA92730; T478_0555.
DR   GeneID; 24816449; -.
DR   KEGG; nbv:T478_0555; -.
DR   KO; K22699; -.
DR   OrthoDB; 61905at2157; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000030944; Chromosome.
DR   Proteomes; UP000241022; 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:UP000030944,
KW   ECO:0000313|Proteomes:UP000241022};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Isomerase {ECO:0000313|EMBL:PTL87822.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00304};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030944};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00304};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   NP_BIND      69     70       NAD. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       172    172       Iron; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   METAL       187    187       Iron. {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      50     50       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING      77     77       NAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
FT   BINDING     172    172       NAD; shared with adjacent protomer.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     234    234       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00304}.
FT   BINDING     244    244       Glycine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00304}.
SQ   SEQUENCE   276 AA;  30283 MW;  D1146AE3C2F50D25 CRC64;
     MQESVNEQRP DKIFADAKEV EITRAIAKEF YDVLQDRAES DIIIIGAGPA GLTASRELSL
     MGYKVLVIEQ NNYLGGGYWL GGYMMNPVTV RAPAQKIWDE LGIPYKKVGE GLYLTPGPHA
     VSKLIGAACD AGVKFLNLTK FDDLVMRHGR VAGIVVNWMP VSALPRNITC VDPVALEAKM
     IIDASGHDSV AVKRLVDRQL VEWKGMNPMW VEDGEEHVVH KTGEIYPGLV AAGMSVTETH
     GLARMGPTFG SMLYSGKRAA EVTDQKIKEF ENQIPK
//
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