NMT1_UROFA
ID NMT1_UROFA Reviewed; 341 AA.
AC O00057;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase {ECO:0000250|UniProtKB:P43534};
DE Short=HMP-P synthase {ECO:0000250|UniProtKB:P43534};
DE Short=Hydroxymethylpyrimidine phosphate synthase {ECO:0000250|UniProtKB:P43534};
DE EC=2.-.-.- {ECO:0000250|UniProtKB:P43534};
DE AltName: Full=Planta-induced rust protein 1 {ECO:0000303|PubMed:9150592};
DE AltName: Full=Thiamine biosynthesis protein 1 {ECO:0000303|PubMed:10830262};
DE AltName: Full=Thiamine pyrimidine synthase {ECO:0000250|UniProtKB:C4YMW2};
GN Name=PIG1 {ECO:0000303|PubMed:9150592};
GN Synonyms=THI1 {ECO:0000303|PubMed:10830262};
OS Uromyces fabae (Rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Uromyces.
OX NCBI_TaxID=55588;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=I2; TISSUE=Haustorium;
RX PubMed=9150592; DOI=10.1094/mpmi.1997.10.4.427;
RA Hahn M., Mendgen K.;
RT "Characterization of in planta-induced rust genes isolated from a
RT haustorium-specific cDNA library.";
RL Mol. Plant Microbe Interact. 10:427-437(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, AND DEVELOPMENTAL STAGE.
RX PubMed=10830262; DOI=10.1094/mpmi.2000.13.6.629;
RA Sohn J., Voegele R.T., Mendgen K., Hahn M.;
RT "High level activation of vitamin B1 biosynthesis genes in haustoria of the
RT rust fungus Uromyces fabae.";
RL Mol. Plant Microbe Interact. 13:629-636(2000).
CC -!- FUNCTION: Responsible for the formation of the pyrimidine heterocycle
CC in the thiamine biosynthesis pathway. Catalyzes the formation of
CC hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal
CC phosphate (PLP). The protein uses PLP and the active site histidine to
CC form HMP-P, generating an inactive enzyme. The enzyme can only undergo
CC a single turnover, which suggests it is a suicide enzyme.
CC {ECO:0000250|UniProtKB:P43534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(3+) + 4 H2O + L-histidyl-[4-amino-5-hydroxymethyl-2-
CC methylpyrimidine phosphate synthase] + N(6)-(pyridoxal phosphate)-L-
CC lysyl-[4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase]
CC = (2S)-2-amino-5-hydroxy-4-oxopentanoyl-[4-amino-5-hydroxymethyl-2-
CC methylpyrimidine phosphate synthase] + 3-oxopropanoate + 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + 2 Fe(2+) + 2 H(+) + L-lysyl-
CC [4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase];
CC Xref=Rhea:RHEA:65756, Rhea:RHEA-COMP:16892, Rhea:RHEA-COMP:16893,
CC Rhea:RHEA-COMP:16894, Rhea:RHEA-COMP:16895, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:29979, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:143915, ChEBI:CHEBI:157692;
CC Evidence={ECO:0000250|UniProtKB:P43534};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757;
CC Evidence={ECO:0000250|UniProtKB:P43534};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000250|UniProtKB:P43534};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000305|PubMed:10830262}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P43534}.
CC -!- DEVELOPMENTAL STAGE: Haustoria and rust-infected leaves. Also observed,
CC at lower levels, in spores or hyphae formed in vitro.
CC {ECO:0000269|PubMed:10830262, ECO:0000269|PubMed:9150592}.
CC -!- SIMILARITY: Belongs to the NMT1/THI5 family. {ECO:0000305}.
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DR EMBL; U81789; AAB39877.1; -; mRNA.
DR EMBL; AJ250426; CAB59855.1; -; Genomic_DNA.
DR AlphaFoldDB; O00057; -.
DR SMR; O00057; -.
DR PRIDE; O00057; -.
DR UniPathway; UPA00060; -.
DR GO; GO:0106344; F:4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity from histidine and PLP; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR027939; NMT1/THI5.
DR InterPro; IPR015168; SsuA/THI5.
DR PANTHER; PTHR31528; PTHR31528; 1.
DR Pfam; PF09084; NMT1; 1.
PE 2: Evidence at transcript level;
KW Iron; Metal-binding; Pyridoxal phosphate; Thiamine biosynthesis;
KW Transferase.
FT CHAIN 1..341
FT /note="4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate
FT synthase"
FT /id="PRO_0000211623"
FT MOTIF 195..199
FT /note="CCCFC; essential for catalytic activity, may be the
FT site of iron coordination"
FT /evidence="ECO:0000250|UniProtKB:P43534"
FT ACT_SITE 66
FT /evidence="ECO:0000250|UniProtKB:P43534"
FT BINDING 115..118
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P43534"
FT MOD_RES 62
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43534"
SQ SEQUENCE 341 AA; 37706 MW; B336BDBF82A0D40A CRC64;
MSTDKISVLL NWHATPYHLP IFVAQSKGFF AKEGIKVAIL EPNDPSDVTE LIGSGKADLG
CKAMIHTLAG KARGFPIKSI GTLMDEPFTG VIYLEGSGIT SDFRSLKGKR IGYVGEFGKI
QIDELTKYYG MTSKDYTAVR CGMNVSKAII EGTIDAGIGL ENIQQVELEE WCKANNRPAS
DVKMLRIDEL AELGCCCFCS ILYIANEDWL KDHPKETAAF MRAVKAGADA MFADPRGSWA
EYCKVKPAMN TPLNRIMFDR SFNYMSQDLI NVSRDWNKVT NYSKRLGIVP EDFVSNYTNE
FVQWEVAPEG GEAEGLAKQQ EMKTLQAHVA EHGGVLQAVT A
