THI4_AERPE
ID THI4_AERPE Reviewed; 270 AA.
AC Q9Y9Z0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Thiamine thiazole synthase {ECO:0000255|HAMAP-Rule:MF_00304};
DE EC=2.4.2.60 {ECO:0000255|HAMAP-Rule:MF_00304};
GN Name=thi4 {ECO:0000255|HAMAP-Rule:MF_00304}; OrderedLocusNames=APE_2149.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00304}.
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_00304};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00304};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00304}.
CC -!- SUBUNIT: Homooctamer; tetramer of dimers. {ECO:0000255|HAMAP-
CC Rule:MF_00304}.
CC -!- PTM: During the catalytic reaction, a sulfide is transferred from Cys-
CC 159 to a reaction intermediate, generating a dehydroalanine residue.
CC {ECO:0000255|HAMAP-Rule:MF_00304}.
CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000255|HAMAP-
CC Rule:MF_00304}.
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DR EMBL; BA000002; BAA81160.2; -; Genomic_DNA.
DR PIR; H72521; H72521.
DR AlphaFoldDB; Q9Y9Z0; -.
DR SMR; Q9Y9Z0; -.
DR STRING; 272557.APE_2149.1; -.
DR EnsemblBacteria; BAA81160; BAA81160; APE_2149.1.
DR KEGG; ape:APE_2149.1; -.
DR PATRIC; fig|272557.25.peg.1430; -.
DR eggNOG; arCOG00574; Archaea.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002518; Chromosome.
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:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00304; Thi4; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR002922; Thi4_fam.
DR InterPro; IPR022828; Thi4_prok.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00292; TIGR00292; 1.
PE 3: Inferred from homology;
KW Iron; Metal-binding; NAD; Reference proteome; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..270
FT /note="Thiamine thiazole synthase"
FT /id="PRO_0000153943"
FT BINDING 39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 58..59
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 66
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="ligand shared between two adjacent protomers"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT BINDING 233
FT /ligand="glycine"
FT /ligand_id="ChEBI:CHEBI:57305"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
FT MOD_RES 159
FT /note="2,3-didehydroalanine (Cys)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00304"
SQ SEQUENCE 270 AA; 28554 MW; 0A04A91F83D4C1E2 CRC64;
MVFARVNEAD VTEAILDGFY SSLKKHLRSD VIVVGAGPAG LTAAWRLAEA GARVLIVEQN
NYLGGGLWLG GYFMNPVTIR APAQRILDEL EVPYEAVKPG LYRTKGPLLA AKLAARALEA
GAEVLNLTML DDVIVENSRV AGVVVNWSPV QGLPRQITCV DPVGLRAEYV VDATGHDAVV
TRKLAERGMV EASKLGPMWV ERSEDLVVEK TGEVYPGLVV AGIAVAEVYG LPRMGPTFGA
MLLSGEKAAA LIGEKLGLKV KVAAAPASQA
