ID A0A0D2C141_9EURO Unreviewed; 341 AA.
AC A0A0D2C141;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase {ECO:0000256|RuleBase:RU367015};
DE Short=HMP-P synthase {ECO:0000256|RuleBase:RU367015};
DE Short=Hydroxymethylpyrimidine phosphate synthase {ECO:0000256|RuleBase:RU367015};
GN ORFNames=PV05_02974 {ECO:0000313|EMBL:KIW58461.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW58461.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW58461.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW58461.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003469, ECO:0000256|RuleBase:RU367015}.
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:0000256|ARBA:ARBA00023967};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65757;
CC Evidence={ECO:0000256|ARBA:ARBA00023967};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|RuleBase:RU367015};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948, ECO:0000256|RuleBase:RU367015}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU367015}.
CC -!- SIMILARITY: Belongs to the NMT1/THI5 family.
CC {ECO:0000256|ARBA:ARBA00009406, ECO:0000256|RuleBase:RU367015}.
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DR EMBL; KN847318; KIW58460.1; -; Genomic_DNA.
DR EMBL; KN847318; KIW58461.1; -; Genomic_DNA.
DR EMBL; KN847318; KIW58462.1; -; Genomic_DNA.
DR RefSeq; XP_013319044.1; XM_013463590.1.
DR RefSeq; XP_013319045.1; XM_013463591.1.
DR RefSeq; XP_013319046.1; XM_013463592.1.
DR STRING; 348802.A0A0D2C141; -.
DR GeneID; 25324882; -.
DR HOGENOM; CLU_028871_6_3_1; -.
DR OrthoDB; 45357at2759; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13650; PBP2_THI5; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR027939; NMT1/THI5.
DR InterPro; IPR015168; SsuA/THI5.
DR PANTHER; PTHR31528; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR PANTHER; PTHR31528:SF1; 4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE PHOSPHATE SYNTHASE THI11-RELATED; 1.
DR Pfam; PF09084; NMT1; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU367015};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU367015};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977,
KW ECO:0000256|RuleBase:RU367015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..238
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 341 AA; 38314 MW; EF1BD1B62E235CDB CRC64;
MSSDKIVFLT NWHATPYHAP LYLAQAKGYF KDEGVQVALL EPNDPSDVTE IIGTGKADLG
YKAMIHTLAA KARGFPVQSI GSLLDEPFTG VVYLKSSGIT TDFRTLKGKR IGYVGEFGKI
QIDELTSHYG MSPTDYTAIR CGMNVSKAII EGTIDAGIGL ENVQMVELED WLESQGRPKS
DVQMLRIDEL AELGCCCFCT ILYIGNEAFL AENPKKVSAF MSAVKRATDF MLRDPEAAWR
EYTDFKPVMN TPLNRKMYER SFPYFSVDLK NVRRDWDKVT AYGKRLGVLE KDFRPNYTND
FLGWKLEGES QDPTGDQKRM VDLQCKIRTT GGLRRLEAVT A
//
