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Database: UniProt
Entry: A0A0B0N4J4_GOSAR
LinkDB: A0A0B0N4J4_GOSAR
Original site: A0A0B0N4J4_GOSAR 
ID   A0A0B0N4J4_GOSAR        Unreviewed;       357 AA.
AC   A0A0B0N4J4;
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, chloroplastic {ECO:0000256|HAMAP-Rule:MF_03158};
DE   AltName: Full=Thiazole biosynthetic enzyme {ECO:0000256|HAMAP-Rule:MF_03158};
DE            EC=2.4.2.60 {ECO:0000256|HAMAP-Rule:MF_03158};
GN   Name=THI1 {ECO:0000256|HAMAP-Rule:MF_03158};
GN   ORFNames=F383_09790 {ECO:0000313|EMBL:KHG06769.1};
OS   Gossypium arboreum (Tree cotton) (Gossypium nanking).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Malvales; Malvaceae; Malvoideae;
OC   Gossypium.
OX   NCBI_TaxID=29729 {ECO:0000313|EMBL:KHG06769.1};
RN   [1] {ECO:0000313|EMBL:KHG06769.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mudge J., Ramaraj T., Lindquist I.E., Bharti A.K., Sundararajan A.,
RA   Cameron C.T., Woodward J.E., May G.D., Brubaker C., Broadhvest J.,
RA   Wilkins T.A.;
RT   "G. arboreum L. cv. AKA8401 A2 genome assembly version 1.0.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in biosynthesis of the thiamine precursor
CC       thiazole. Catalyzes the conversion of NAD and glycine to adenosine
CC       diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid
CC       (ADT), an adenylated thiazole intermediate. The reaction includes
CC       an iron-dependent sulfide transfer from a conserved cysteine
CC       residue of the protein to a thiazole intermediate. The enzyme can
CC       only undergo a single turnover, which suggests it is a suicide
CC       enzyme. May have additional roles in adaptation to various stress
CC       conditions and in DNA damage tolerance. {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) =
CC         [ADP-thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-
CC         methylthiazole-2-carboxylate + 2 H(+) + 3 H2O + nicotinamide;
CC         Xref=Rhea:RHEA:55708, Rhea:RHEA-COMP:14264, Rhea:RHEA-
CC         COMP:14265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:90873, ChEBI:CHEBI:139151;
CC         EC=2.4.2.60; Evidence={ECO:0000256|HAMAP-Rule:MF_03158};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03158};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03158};
CC   -!- SUBUNIT: Homooctamer. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
CC   -!- PTM: During the catalytic reaction, a sulfide is transferred from
CC       Cys-224 to a reaction intermediate, generating a dehydroalanine
CC       residue. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC   -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000256|HAMAP-
CC       Rule:MF_03158}.
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:KHG06769.1}.
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DR   EMBL; JRRC01459852; KHG06769.1; -; Genomic_DNA.
DR   RefSeq; XP_017640755.1; XM_017785266.1.
DR   GeneID; 108482152; -.
DR   KEGG; gab:108482152; -.
DR   KO; K03146; -.
DR   OMA; MWGGGMM; -.
DR   OrthoDB; 1111148at2759; -.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-UniRule.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
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:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_03158; THI4; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027495; Sti35.
DR   InterPro; IPR002922; Thi4_fam.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR00292; TIGR00292; 1.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_03158};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Plastid {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      122    123       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      303    305       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING     102    102       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     130    130       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     195    195       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     226    226       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     241    241       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     293    293       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     224    224       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   357 AA;  38117 MW;  CB08BADEE61A867D CRC64;
     MASSMATTLT SSSKLCRNTS LFESSFHGVP IKPLSFHFKT KSSHCNASIS MSAASPPPYD
     FNNFRFDPIK ESIVSREMTR RYMMDMIIYA DTDVVVVGAG SAGLSCAYEL SKNPSVQIAI
     VEQSVSPGGG AWLGGQLFSA MVVRKPAHRF LDELAIEYDE QDDYVVIKHA ALFTSTIMSK
     LLARPNVKLF NAVAAEDLIV KEGRVGGIVT NWALVSMNHD TQSCMDPNVM EAKVVVSSCG
     HDGPFGATGV KRLKSIGMID SVPGMKALDM NTAEDAIVRL TREIVPGMIV TGMEVAEIDG
     SPRMGPTFGA MMISGQKAAH LALKSLGLPN AIDGTHVGTI HPELILAVAD SAETADA
//
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