THIC_ECOLI
ID THIC_ECOLI Reviewed; 631 AA.
AC P30136; Q2M8T1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 160.
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};
GN OrderedLocusNames=b3994, JW3958;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8432721; DOI=10.1128/jb.175.4.982-992.1993;
RA Vander Horn P.B., Backstrom A.D., Stewart V., Begley T.P.;
RT "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in
RT Escherichia coli K-12.";
RL J. Bacteriol. 175:982-992(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP FUNCTION IN THIAMINE METABOLISM.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15292217; DOI=10.1074/jbc.m404284200;
RA Lawhorn B.G., Gerdes S.Y., Begley T.P.;
RT "A genetic screen for the identification of thiamin metabolic genes.";
RL J. Biol. Chem. 279:43555-43559(2004).
RN [5]
RP FUNCTION IN AIR CONVERSION.
RC STRAIN=K12;
RX PubMed=15326535; DOI=10.1039/b405429f;
RA Lawhorn B.G., Mehl R.A., Begley T.P.;
RT "Biosynthesis of the thiamin pyrimidine: the reconstitution of a remarkable
RT rearrangement reaction.";
RL Org. Biomol. Chem. 2:2538-2546(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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:0000305|PubMed:15292217, ECO:0000305|PubMed:15326535}.
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; M88701; AAB95616.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43092.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76968.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77325.1; -; Genomic_DNA.
DR PIR; E65206; E65206.
DR RefSeq; NP_418422.1; NC_000913.3.
DR RefSeq; WP_001276926.1; NZ_STEB01000045.1.
DR AlphaFoldDB; P30136; -.
DR SMR; P30136; -.
DR BioGRID; 4259335; 9.
DR DIP; DIP-10982N; -.
DR IntAct; P30136; 7.
DR STRING; 511145.b3994; -.
DR PaxDb; P30136; -.
DR PRIDE; P30136; -.
DR EnsemblBacteria; AAC76968; AAC76968; b3994.
DR EnsemblBacteria; BAE77325; BAE77325; BAE77325.
DR GeneID; 66672094; -.
DR GeneID; 948492; -.
DR KEGG; ecj:JW3958; -.
DR KEGG; eco:b3994; -.
DR PATRIC; fig|1411691.4.peg.2717; -.
DR EchoBASE; EB1544; -.
DR eggNOG; COG0422; Bacteria.
DR HOGENOM; CLU_013181_2_1_6; -.
DR InParanoid; P30136; -.
DR OMA; TWELFRD; -.
DR PhylomeDB; P30136; -.
DR BioCyc; EcoCyc:THIC-MON; -.
DR BioCyc; MetaCyc:THIC-MON; -.
DR UniPathway; UPA00060; -.
DR PRO; PR:P30136; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding; Reference proteome;
KW S-adenosyl-L-methionine; Thiamine biosynthesis; Zinc.
FT CHAIN 1..631
FT /note="Phosphomethylpyrimidine synthase"
FT /id="PRO_0000152804"
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"
FT CONFLICT 623..630
FT /note="EIYLRKEE -> RNLP (in Ref. 1; AAB95616)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 631 AA; 70850 MW; 6F2105B4792CBA3F CRC64;
MSATKLTRRE QRARAQHFID TLEGTAFPNS KRIYITGTHP GVRVPMREIQ LSPTLIGGSK
EQPQYEENEA IPVYDTSGPY GDPQIAINVQ QGLAKLRQPW IDARGDTEEL TVRSSDYTKA
RLADDGLDEL RFSGVLTPKR AKAGRRVTQL HYARQGIITP EMEFIAIREN MGRERIRSEV
LRHQHPGMSF GAHLPENITA EFVRDEVAAG RAIIPANINH PESEPMIIGR NFLVKVNANI
GNSAVTSSIE EEVEKLVWST RWGADTVMDL STGRYIHETR EWILRNSPVP IGTVPIYQAL
EKVNGIAEDL TWEAFRDTLL EQAEQGVDYF TIHAGVLLRY VPMTAKRLTG IVSRGGSIMA
KWCLSHHQEN FLYQHFREIC EICAAYDVSL SLGDGLRPGS IQDANDEAQF AELHTLGELT
KIAWEYDVQV MIEGPGHVPM QMIRRNMTEE LEHCHEAPFY TLGPLTTDIA PGYDHFTSGI
GAAMIGWFGC AMLCYVTPKE HLGLPNKEDV KQGLITYKIA AHAADLAKGH PGAQIRDNAM
SKARFEFRWE DQFNLALDPF TARAYHDETL PQESGKVAHF CSMCGPKFCS MKISQEVRDY
AATQTIEMGM ADMSENFRAR GGEIYLRKEE A
