THI43_PHYPA
ID THI43_PHYPA Reviewed; 357 AA.
AC A9RHW6;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Thiamine thiazole synthase 3, 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 3 {ECO:0000255|HAMAP-Rule:MF_03158};
DE Flags: Precursor;
GN Name=THI1-3 {ECO:0000255|HAMAP-Rule:MF_03158};
GN ORFNames=PHYPADRAFT_114476, PHYPADRAFT_114591;
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
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 -!- 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 -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 225 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000255|HAMAP-Rule:MF_03158}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_03158}.
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DR EMBL; DS544899; EDQ81450.1; -; Genomic_DNA.
DR EMBL; DS544899; EDQ81452.1; -; Genomic_DNA.
DR RefSeq; XP_001753698.1; XM_001753646.1.
DR RefSeq; XP_001753700.1; XM_001753648.1.
DR AlphaFoldDB; A9RHW6; -.
DR SMR; A9RHW6; -.
DR STRING; 3218.PP1S10_341V6.1; -.
DR EnsemblPlants; Pp3c23_6580V3.2; Pp3c23_6580V3.2; Pp3c23_6580.
DR Gramene; Pp3c23_6580V3.2; Pp3c23_6580V3.2; Pp3c23_6580.
DR eggNOG; KOG2960; Eukaryota.
DR HOGENOM; CLU_308926_0_0_1; -.
DR InParanoid; A9RHW6; -.
DR Proteomes; UP000006727; Chromosome 23.
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 3: Inferred from homology;
KW Chloroplast; Iron; Metal-binding; NAD; Plastid; Reference proteome;
KW Thiamine biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT CHAIN 52..357
FT /note="Thiamine thiazole synthase 3, chloroplastic"
FT /id="PRO_0000415863"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 123..124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT BINDING 304..306
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
FT MOD_RES 225
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03158"
SQ SEQUENCE 357 AA; 37873 MW; 0930AE3068CA06B9 CRC64;
MSISAAGVAT GLGANVELKS NVGSSSSSVA GVRLFTSRKA QLRRCAAPAT SASLYSDANY
DLNNYKFAPI KESIVAREMT RRYMTDMITH ADTDVVVVGA GSAGLSCAYE LSKNPNVKVA
IVEQSVSPGG GAWLGGQLFS AMIVRKPAHR FLDEIEVPYE EMENYVVIKH AALFTSTIMS
KLLARPNVKL FNAVAAEDLI IRGDRVSGVV TNWALVAQNH NTQSCMDPNV MEAKVVVSSC
GHDGPFGATG VKRLRSIGMI ESVPGMKCLD MNAAEDAIVK HTREVVPGMI VTGMEVAEID
GSPRMGPTFG AMMISGQKAA HLALRALGLP NEVDGNYKPN VHPELVLAST DDMTASA
