THIEC_BIFLO
ID THIEC_BIFLO Reviewed; 917 AA.
AC Q8G7X1;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Thiamine biosynthesis bifunctional protein ThiEC;
DE Includes:
DE RecName: Full=Thiamine-phosphate synthase;
DE Short=TMP-PPase;
DE Short=TP synthase;
DE Short=TPS;
DE EC=2.5.1.3 {ECO:0000250|UniProtKB:P39594};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase;
DE Short=TMP pyrophosphorylase;
DE Includes:
DE RecName: Full=Phosphomethylpyrimidine synthase;
DE EC=4.1.99.17 {ECO:0000250|UniProtKB:P45740};
DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase;
DE Short=HMP-P synthase;
DE Short=HMP-phosphate synthase;
DE Short=HMPP synthase;
DE AltName: Full=Thiamine biosynthesis protein ThiC;
GN Name=thiE/thiC; OrderedLocusNames=BL0114;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine
CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC {ECO:0000250|UniProtKB:P39594}.
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:0000250|UniProtKB:P45740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000250|UniProtKB:P39594};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000250|UniProtKB:P39594};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3;
CC Evidence={ECO:0000250|UniProtKB:P39594};
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:0000250|UniProtKB:P45740};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
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:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC -!- SIMILARITY: In the N-terminal section; belongs to the thiamine-
CC phosphate synthase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiC family.
CC {ECO:0000305}.
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DR EMBL; AE014295; AAN23979.1; -; Genomic_DNA.
DR RefSeq; NP_695343.1; NC_004307.2.
DR RefSeq; WP_011067965.1; NC_004307.2.
DR AlphaFoldDB; Q8G7X1; -.
DR SMR; Q8G7X1; -.
DR STRING; 206672.BL0114; -.
DR PRIDE; Q8G7X1; -.
DR EnsemblBacteria; AAN23979; AAN23979; BL0114.
DR KEGG; blo:BL0114; -.
DR PATRIC; fig|206672.9.peg.122; -.
DR HOGENOM; CLU_013181_0_1_11; -.
DR OMA; KEWRGRT; -.
DR PhylomeDB; Q8G7X1; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000000439; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-UniRule.
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 CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.540; -; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00089; ThiC; 1.
DR HAMAP; MF_00097; TMP_synthase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR037509; ThiC.
DR InterPro; IPR025747; ThiC-associated_dom.
DR InterPro; IPR038521; ThiC/Bza_core_dom.
DR InterPro; IPR002817; ThiC/BzaA/B.
DR InterPro; IPR034291; TMP_synthase.
DR PANTHER; PTHR30557; PTHR30557; 1.
DR Pfam; PF13667; ThiC-associated; 1.
DR Pfam; PF01964; ThiC_Rad_SAM; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SFLD; SFLDF00407; phosphomethylpyrimidine_syntha; 1.
DR SUPFAM; SSF51391; SSF51391; 1.
DR TIGRFAMs; TIGR00190; thiC; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Lyase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Reference proteome; S-adenosyl-L-methionine;
KW Thiamine biosynthesis; Transferase; Zinc.
FT CHAIN 1..917
FT /note="Thiamine biosynthesis bifunctional protein ThiEC"
FT /id="PRO_0000152856"
FT REGION 1..243
FT /note="Thiamine-phosphate synthase"
FT REGION 256..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..917
FT /note="Phosphomethylpyrimidine synthase"
FT COMPBIAS 276..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 48..52
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 157..159
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine"
FT /ligand_id="ChEBI:CHEBI:57841"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 216..217
FT /ligand="2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-
FT ylidene]ethyl phosphate"
FT /ligand_id="ChEBI:CHEBI:62899"
FT /evidence="ECO:0000250"
FT BINDING 487
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 545
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 581
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 601..603
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 642..645
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 681
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="5-amino-1-(5-phospho-beta-D-ribosyl)imidazole"
FT /ligand_id="ChEBI:CHEBI:137981"
FT /evidence="ECO:0000250"
FT BINDING 749
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 829
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 832
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 837
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
SQ SEQUENCE 917 AA; 100355 MW; 00000DA28A98E1F6 CRC64;
MSNEYPYASM RDSFDLSAYF VVGPEDCKGR PLTDVVDQAL HGGATFIQLR AKEADASELT
DMARDIAQII EDNEKSDSVA FVIDDRADVV WQARRKGIKV DGVHIGQTDM EPREARALLG
DEAIVGLSAE TESLVRLINE LPDGCIDYIG AGPLHVSTTK PEASVGGNDG SGKTLDAAQI
NTICVASEFP VVVGGGVTAA DMAMLADTKA AGWFVVSAIA GAENPEEAAR TMVEGWKAVR
GDKKHGYAPR VVTHTPATDT QAAQEGAAKP GSEATEKKFT NAKDAKDAQK LAKQQRVDIA
ARGSKQRDKA HIRKTKSVPF TYQYGSYDLE VPYTEIKLSD TPGVGPNPPF HDYNTEGPKC
DPKEGLKPLR LDWIRDRGDI EDYEGRRRNL EDDGKRAIKR GRATKEWRGR KHEPMRAKDH
PITQMWYARH GIITPEMQYV ATRENCDVEL VRSELAAGRA VMPCNINHPE AEPMIIGSAF
LTKLNANMGN SAVTSSIDEE VEKLTWATKW GADTVMDLST GNDIHTTREW ILRNSPVPIG
TVPMYQALEK VEDDASKLSW ELFRDTVIEQ CEQGVDYMTI HAGVLLRYVP LTANRVTGIV
SRGGSIMADW CLRHHQESFL YTHFDELCDI FAKYDVAFSL GDGLRPGSLA DANDAAQLSE
LMTLGELTER AWAKDVQVMI EGPGHVPFDT VRMNIELEKA VCHNAPFYTL GPLTTDTAPG
YDHITSAIGA TEIGRYGTAM LCYVTPKEHL GLPNKDDVKQ GVIAYKIACH AADIAKHHPH
AMDRDNAISK ARFEFRWLDQ FNLSYDPDTA IAFHDDTLPA EPAKMAHFCS MCGPKFCSMA
ISQNIRKAFG GEAAQQQIVK EAAAGIDSEA LATAKANVDN GVVSANVLSP EEILAGMDAM
SEKYTAQGGK LYSTAQE
