GenomeNet

Database: UniProt
Entry: A0A2H3YT24_PHODC
LinkDB: A0A2H3YT24_PHODC
Original site: A0A2H3YT24_PHODC 
ID   A0A2H3YT24_PHODC        Unreviewed;       355 AA.
AC   A0A2H3YT24;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   03-JUL-2019, entry version 10.
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=LOC103716822 {ECO:0000313|RefSeq:XP_008803216.1};
GN   Synonyms=THI1 {ECO:0000256|HAMAP-Rule:MF_03158};
OS   Phoenix dactylifera (Date palm).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Arecaceae; Coryphoideae;
OC   Phoeniceae; Phoenix.
OX   NCBI_TaxID=42345 {ECO:0000313|Proteomes:UP000228380, ECO:0000313|RefSeq:XP_008803216.1};
RN   [1] {ECO:0000313|Proteomes:UP000228380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Khalas {ECO:0000313|Proteomes:UP000228380};
RX   PubMed=23917264; DOI=10.1038/ncomms3274;
RA   Al-Mssallem I.S., Hu S., Zhang X., Lin Q., Liu W., Tan J., Yu X.,
RA   Liu J., Pan L., Zhang T., Yin Y., Xin C., Wu H., Zhang G.,
RA   Ba Abdullah M.M., Huang D., Fang Y., Alnakhli Y.O., Jia S., Yin A.,
RA   Alhuzimi E.M., Alsaihati B.A., Al-Owayyed S.A., Zhao D., Zhang S.,
RA   Al-Otaibi N.A., Sun G., Majrashi M.A., Li F., Tala, Wang J., Yun Q.,
RA   Alnassar N.A., Wang L., Yang M., Al-Jelaify R.F., Liu K., Gao S.,
RA   Chen K., Alkhaldi S.R., Liu G., Zhang M., Guo H., Yu J.;
RT   "Genome sequence of the date palm Phoenix dactylifera L.";
RL   Nat. Commun. 4:2274-2274(2013).
RN   [2] {ECO:0000313|RefSeq:XP_008803216.1}
RP   IDENTIFICATION.
RC   TISSUE=Bud {ECO:0000313|RefSeq:XP_008803216.1};
RG   RefSeq;
RL   Submitted (MAR-2019) to UniProtKB.
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-221 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   -----------------------------------------------------------------------
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   RefSeq; XP_008803216.1; XM_008804994.1.
DR   GeneID; 103716822; -.
DR   KEGG; pda:103716822; -.
DR   KO; K03146; -.
DR   OrthoDB; 1111148at2759; -.
DR   Proteomes; UP000228380; Genome assembly.
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   Complete proteome {ECO:0000313|Proteomes:UP000228380};
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   Reference proteome {ECO:0000313|Proteomes:UP000228380};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_03158};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   REGION      119    120       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   REGION      300    302       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03158}.
FT   BINDING      99     99       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     127    127       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   BINDING     192    192       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     238    238       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03158}.
FT   BINDING     290    290       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
FT   MOD_RES     221    221       2,3-didehydroalanine (Cys).
FT                                {ECO:0000256|HAMAP-Rule:MF_03158}.
SQ   SEQUENCE   355 AA;  37546 MW;  48D539F31A3AB76A CRC64;
     MATMATSTLA AKPKTSFVDH YHSSFSGLIL PSRVSATRSH SSPSLSISAS AAAPRYDLNS
     IRFNPIKESI VSREMTRRYM TDMITHADTD VVVIGAGSAG LSCAYELSKD PSVCVAIVEQ
     SVSPGGGAWL GGQLFSAMVV RKPAHLFLDE LGIPYDEQDS YVVIKHAALF TSTIMSRLLA
     RPNVKLFNAV AAEGLIVKEG RVAGVVTNWA LVSMNHDTQS CMDPNVMEAK VVVSSCGHDG
     PFGATGVKRL KDIGMIDSVP GMKALDMNSA EDAIVRLTRE IVPGMIVTGM EVAEIDGAPR
     MGPTFGAMMI SGQKAAHLAL KALGRPNALD GISWAEKVHP EMVLASSEGG DVVDA
//
DBGET integrated database retrieval system