ID   THIC_SALG2              Reviewed;         631 AA.
AC   B5RFJ0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            EC=4.1.99.17 {ECO:0000255|HAMAP-Rule:MF_00089};
DE   AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMP-P synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMP-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE            Short=HMPP synthase {ECO:0000255|HAMAP-Rule:MF_00089};
DE   AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000255|HAMAP-Rule:MF_00089};
GN   Name=thiC {ECO:0000255|HAMAP-Rule:MF_00089}; OrderedLocusNames=SG3442;
OS   Salmonella gallinarum (strain 287/91 / NCTC 13346).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=287/91 / NCTC 13346;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
CC   -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine
CC       phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR)
CC       in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
CC       {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-
CC         methionine = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + 5'-
CC         deoxyadenosine + CO + formate + 3 H(+) + L-methionine;
CC         Xref=Rhea:RHEA:24840, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:17245, ChEBI:CHEBI:17319, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:58354, ChEBI:CHEBI:59789, ChEBI:CHEBI:137981;
CC         EC=4.1.99.17; Evidence={ECO:0000255|HAMAP-Rule:MF_00089};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00089};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated
CC       with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000255|HAMAP-Rule:MF_00089};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00089}.
CC   -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP-
CC       Rule:MF_00089}.
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DR   EMBL; AM933173; CAR39233.1; -; Genomic_DNA.
DR   RefSeq; WP_000108430.1; NC_011274.1.
DR   AlphaFoldDB; B5RFJ0; -.
DR   SMR; B5RFJ0; -.
DR   EnsemblBacteria; CAR39233; CAR39233; SG3442.
DR   KEGG; seg:SG3442; -.
DR   HOGENOM; CLU_013181_2_1_6; -.
DR   OMA; TWELFRD; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000008321; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; 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   Gene3D; 3.20.20.540; -; 1.
DR   HAMAP; MF_00089; ThiC; 1.
DR   InterPro; IPR037509; ThiC.
DR   InterPro; IPR025747; ThiC-associated_dom.
DR   InterPro; IPR038521; ThiC/Bza_core_dom.
DR   InterPro; IPR002817; ThiC/BzaA/B.
DR   PANTHER; PTHR30557; PTHR30557; 1.
DR   Pfam; PF13667; ThiC-associated; 1.
DR   Pfam; PF01964; ThiC_Rad_SAM; 1.
DR   SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
DR   TIGRFAMs; TIGR00190; thiC; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; S-adenosyl-L-methionine;
KW   Thiamine biosynthesis; Zinc.
FT   CHAIN           1..631
FT                   /note="Phosphomethylpyrimidine synthase"
FT                   /id="PRO_1000093230"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         353..355
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         394..397
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         433
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         437
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         460
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         501
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         581
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         584
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
FT   BINDING         589
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00089"
SQ   SEQUENCE   631 AA;  70722 MW;  F0829B1F280BB67A CRC64;
     MSTTTLTRRE QRAKAQHFID TLEGTAFPNS KRIYVTGSQH DIRVPMREIQ LSPTLIGGSK
     DNQQFEENEA VPVYDTSGPY GDPEVAINVQ QGLAKLRQPW IDARNDSEEL DDRSSAYTRE
     RLADDGLDDL RFTGLLTPKR AKAGKRITQL HYARQGIVTP EMEFIAIREN MGRERICSEV
     LRHQHPGMSF GARLPENITP EFVRDEVAAG RAIIPANINH PESEPMIIGR NFPVKVNANI
     GNSAVTSSIE EEVEKLVWST RWGADTVMDL STGRYIHETR EWILRNSPVP IGTVPIYQAL
     EKVNGIAEDL TWEAFRDTLL EQAEQGVDYF TIHAGVLLRY VPMTAKRLTG IVSRGGSIMA
     KWCLSHHKEN FLFEHFREIC EICAAYDVSL SLGDGLRPGS IQDANDEAQF SELHTLGELT
     KIAWEYDVQV MIEGPGHVPM HMIQRNMTEE LESCHEAPFY TLGPLTTDIA PGYDHFTSGI
     GAAMIGWFGC AMLCYVTPKE HLGLPNKEDV KQGLITYKIA AHAADLAKGH PGAQIRDNAM
     SKARFEFRWE DQFNLALDPF TARAYHDETL PQESGKVAHF CSMCGPKFCS MKISQEVRDY
     AAAQAIEVGM ADMSESFRAK GGEIYLKREE A