ID A0A2H5PII9_CITUN Unreviewed; 356 AA.
AC A0A2H5PII9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 13-SEP-2023, entry version 20.
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=CUMW_139980 {ECO:0000313|EMBL:GAY52187.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY52187.1};
RN [1] {ECO:0000313|EMBL:GAY52187.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
CC -!- FUNCTION: Involved in biosynthesis of the thiamine precursor thiazole.
CC Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-
CC (2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an
CC adenylated thiazole intermediate. The reaction includes an iron-
CC dependent sulfide transfer from a conserved cysteine residue of the
CC protein to a thiazole intermediate. The enzyme can only undergo a
CC single turnover, which suggests it is a suicide enzyme. May have
CC additional roles in adaptation to various stress conditions and in DNA
CC damage tolerance. {ECO:0000256|HAMAP-Rule:MF_03158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[ADP-thiazole synthase]-L-cysteine + glycine + NAD(+) = [ADP-
CC thiazole synthase]-dehydroalanine + ADP-5-ethyl-4-methylthiazole-2-
CC carboxylate + 2 H(+) + 3 H2O + nicotinamide; Xref=Rhea:RHEA:55708,
CC Rhea:RHEA-COMP:14264, Rhea:RHEA-COMP:14265, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57540, ChEBI:CHEBI:90873,
CC ChEBI:CHEBI:139151; EC=2.4.2.60; Evidence={ECO:0000256|HAMAP-
CC 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-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 Cys-
CC 223 to a reaction intermediate, generating a dehydroalanine residue.
CC {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 EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY52187.1}.
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DR EMBL; BDQV01000078; GAY52187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5PII9; -.
DR STRING; 55188.A0A2H5PII9; -.
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:pentosyltransferase activity; 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; 6.10.250.2840; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR HAMAP; MF_03158; THI4; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR027495; Sti35.
DR InterPro; IPR002922; Thi4_fam.
DR NCBIfam; TIGR00292; sulfide-dependent adenosine diphosphate thiazole synthase; 1.
DR PANTHER; PTHR43422; THIAMINE THIAZOLE SYNTHASE; 1.
DR PANTHER; PTHR43422:SF3; THIAMINE THIAZOLE SYNTHASE; 1.
DR Pfam; PF01946; Thi4; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|HAMAP-Rule:MF_03158};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_03158};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03158}; NAD {ECO:0000256|HAMAP-Rule:MF_03158};
KW Plastid {ECO:0000256|HAMAP-Rule:MF_03158};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_03158}; Transferase {ECO:0000256|HAMAP-Rule:MF_03158}.
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 121..122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT BINDING 302..304
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
FT MOD_RES 223
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03158"
SQ SEQUENCE 356 AA; 37611 MW; 6C6298D4454B01B2 CRC64;
MAAMASTAFA PSVSSTTNKL FDSSFHGAPM SPSLLRLQPI KSSRPNNLSI SASASPPYDL
NTFKFDPIKE SIVSREMTRR YMTDMITYAD TDVVVVGAGS AGLSCAYELS KNPNIQIAII
EQSVSPGGGA WLSGQLFSAM VVRKPAHIFL DELGIDYDEQ DNYVVIKHAA LFTSTIMSKL
LARPNVKLFN AVAAEDLIVK GGRVGGVVTN WALVSMNHDT QSCMDPNVME AKVVVSSCGH
DGPFGATGVK RLKSIGMIEE VPGMKALDMN SAEDAIVRLT REVVPGMIVT GMEVAEIDGA
PRMGPTFGAM MISGQKAAHL ALKSLGQPNA LDGTYVGGVH PELILAAADS AETADG
//
