THI4_ALNGL
ID THI4_ALNGL Reviewed; 352 AA.
AC Q38709;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Thiamine thiazole synthase, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03158};
DE EC=2.4.2.60 {ECO:0000255|HAMAP-Rule:MF_03158};
DE AltName: Full=Thiazole biosynthetic enzyme {ECO:0000255|HAMAP-Rule:MF_03158};
GN Name=THI1 {ECO:0000255|HAMAP-Rule:MF_03158}; Synonyms=AG6, THI4;
OS Alnus glutinosa (European alder) (Betula alnus var. glutinosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fagales; Betulaceae; Alnus.
OX NCBI_TaxID=3517;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Root nodule;
RX PubMed=8771789; DOI=10.1046/j.1365-313x.1996.10020361.x;
RA Ribeiro A., Praekelt U., Akkermans A.D.L., Meacock P.A., van Kammen A.,
RA Bisseling T., Pawlowski K.;
RT "Identification of agthi1, whose product is involved in biosynthesis of the
RT thiamine precursor thiazole, in actinorhizal nodules of Alnus glutinosa.";
RL Plant J. 10:361-368(1996).
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:0000255|HAMAP-Rule:MF_03158,
CC ECO:0000269|PubMed:8771789}.
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:0000255|HAMAP-
CC Rule:MF_03158};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03158};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000255|HAMAP-Rule:MF_03158};
CC -!- SUBUNIT: Homooctamer. {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in nodules and shoot tips,
CC and at low levels in roots, flowers, and developing fruits. In nodules,
CC expressed in the infected cortical cells and in the pericycle of the
CC nodule vascular bundle. {ECO:0000269|PubMed:8771789}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 219 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
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DR EMBL; X97434; CAA66064.1; -; mRNA.
DR AlphaFoldDB; Q38709; -.
DR SMR; Q38709; -.
DR BRENDA; 2.4.2.60; 261.
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; 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 2: Evidence at transcript level;
KW Chloroplast; Iron; Metal-binding; NAD; Plastid; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..352
FT /note="Thiamine thiazole synthase, chloroplastic"
FT /id="PRO_0000034059"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 117..118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 298..300
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT MOD_RES 219
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
SQ SEQUENCE 352 AA; 37065 MW; 635C92AF11CCB070 CRC64;
MASTLTSKPQ RLALFENSAS SFYGTPLAPS SIRVQPTKAG AKPSISMSGA PSPPYDLKAF
TFDPIKESIV SREMTRRYMM DMITYADTDV VVVGAGSSGL VCYELSKNPS VQVAIIEQSV
SPGGGAWLGG QLFSGMVVRK PAHLFLDELG IEYDEQDNYV VIKHAALFTS TIMSKLLARP
NVKLFNAVAA EDLIVKGGRV GGVVTNWALV SMNHDTQSCM DPNVMEAKVV VSSCGHDGPF
GATGVKSLRS IGMIDTVPGM KALDMNVAED AIVRLTREIV PGMIVTGMEV AEIDGAPRMG
PTFGAMMISG QKAAHLALKA LGLPNALDGS YVGGIHPELI LAAADSAEIA DA
