NMT1_SCHPO
ID NMT1_SCHPO Reviewed; 346 AA.
AC P36597;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=No message in thiamine protein 1 {ECO:0000303|PubMed:2358444};
DE AltName: Full=Thiamine biosynthesis protein 3 {ECO:0000303|PubMed:1868574};
DE AltName: Full=Thiamine pyrimidine synthase {ECO:0000250|UniProtKB:C4YMW2};
GN Name=nmt1 {ECO:0000303|PubMed:2358444};
GN Synonyms=thi3 {ECO:0000303|PubMed:1868574};
GN ORFNames=SPCC1223.02 {ECO:0000312|PomBase:SPCC1223.02};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=972 / ATCC 24843;
RX PubMed=2358444; DOI=10.1016/s0021-9258(19)38525-4;
RA Maundrell K.;
RT "nmt1 of fission yeast. A highly transcribed gene completely repressed by
RT thiamine.";
RL J. Biol. Chem. 265:10857-10864(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP GENE NAME.
RX PubMed=1868574; DOI=10.1007/bf00355050;
RA Schweingruber A.M., Dlugonski J., Edenharter E., Schweingruber M.E.;
RT "Thiamine in Schizosaccharomyces pombe: dephosphorylation, intracellular
RT pool, biosynthesis and transport.";
RL Curr. Genet. 19:249-254(1991).
RN [4]
RP INDUCTION.
RX PubMed=1934118; DOI=10.1007/bf00312766;
RA Tommasino M., Maundrell K.;
RT "Uptake of thiamine by Schizosaccharomyces pombe and its effect as a
RT transcriptional regulator of thiamine-sensitive genes.";
RL Curr. Genet. 20:63-66(1991).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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:2358444}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P43534}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- INDUCTION: Repressed by thiamine. {ECO:0000269|PubMed:1934118,
CC ECO:0000269|PubMed:2358444}.
CC -!- DISRUPTION PHENOTYPE: Auxotroph for thiamine.
CC {ECO:0000269|PubMed:2358444}.
CC -!- SIMILARITY: Belongs to the NMT1/THI5 family. {ECO:0000305}.
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DR EMBL; J05493; AAA35318.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20871.1; -; Genomic_DNA.
DR PIR; A42223; A42223.
DR RefSeq; NP_588347.1; NM_001023338.2.
DR AlphaFoldDB; P36597; -.
DR SMR; P36597; -.
DR BioGRID; 275680; 19.
DR STRING; 4896.SPCC1223.02.1; -.
DR iPTMnet; P36597; -.
DR PaxDb; P36597; -.
DR PRIDE; P36597; -.
DR EnsemblFungi; SPCC1223.02.1; SPCC1223.02.1:pep; SPCC1223.02.
DR GeneID; 2539108; -.
DR KEGG; spo:SPCC1223.02; -.
DR PomBase; SPCC1223.02; nmt1.
DR VEuPathDB; FungiDB:SPCC1223.02; -.
DR eggNOG; ENOG502QQ87; Eukaryota.
DR HOGENOM; CLU_028871_6_3_1; -.
DR InParanoid; P36597; -.
DR OMA; DWFVNPD; -.
DR PhylomeDB; P36597; -.
DR UniPathway; UPA00060; -.
DR PRO; PR:P36597; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IMP:PomBase.
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 Cytoplasm; Iron; Metal-binding; Nucleus; Pyridoxal phosphate;
KW Reference proteome; Thiamine biosynthesis; Transferase.
FT CHAIN 1..346
FT /note="4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate
FT synthase"
FT /id="PRO_0000211624"
FT MOTIF 194..198
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 114..117
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 346 AA; 38966 MW; 7B9B9CB0D4087DFC CRC64;
MSTNKITFLT NWEATPYHLP IFLAQTRGYY EREGIEVAIL EPTNPSDVTA LIGSGKVDMG
LKAMIHTLAA KARGYPVTSF GSLLNEPFTG LITLKGNGIN DFKDIKGKRI GYVGEFGKIQ
LDDLCSKFGL SPSDYTAIRC GMNIAPAIIN GEIDGGIGIE CMQQVELERW CVSQGRPRSD
VQMLRIDRLA NLGCCCFCTI LYIAHDEFIA KHPDKIKAFL RAIHSATLDM LKDPVQTYKE
YIHFKREMGS ELHREQFERC FAYFSHDISN VPRDWNKVTN YSKRLGIIPQ DFEPNCTNGY
LTWELDPDEK DPMGKQEAIA EIQDEIKQKG GVFSGNSLRY VEPANL
