ID A0A345DYJ4_9EURY Unreviewed; 330 AA.
AC A0A345DYJ4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN ORFNames=DU500_00430 {ECO:0000313|EMBL:AXG05016.1};
OS Haloplanus rubicundus.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloplanus.
OX NCBI_TaxID=1547898 {ECO:0000313|EMBL:AXG05016.1, ECO:0000313|Proteomes:UP000253273};
RN [1] {ECO:0000313|EMBL:AXG05016.1, ECO:0000313|Proteomes:UP000253273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBA1113 {ECO:0000313|EMBL:AXG05016.1,
RC ECO:0000313|Proteomes:UP000253273};
RA Kim Y.B., Roh S.W.;
RT "Genome sequences of Haloplanus sp. CBA1113.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the NMT1/THI5 family.
CC {ECO:0000256|ARBA:ARBA00009406}.
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DR EMBL; CP031150; AXG05016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345DYJ4; -.
DR KEGG; haj:DU500_00430; -.
DR OrthoDB; 302958at2157; -.
DR Proteomes; UP000253273; Chromosome.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 69..257
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 330 AA; 37418 MW; 071EAB16ECD20E22 CRC64;
MSRDHVDAQQ AALDEYHDDP GDLPTMRARF EHNGSPRYLL YTIKRFGFDH DHGFHLDVQL
VSDALEDGIE TVEAQLQEGH ADLIDIDYIS IARERAEGAD IVAFHPYGRT VGGLVAPEDS
DIEGLEDLSG KRIGVVRRLD KNWILTRAAC REFHDFDPDE TATPVEAGSK VELTRMIEEG
EVDAGFQFWQ IIPEITETGP FENVLPVSEL VQRLSETDDK LPLAAFLTSG EYLDEQRETV
RAFADAYRDA VDKLVEDDEI WEEISEKLMS YDDPDVMRAV RDGWREMVVR DWDDEQVDGM
YRLFDHLKSV AGAEALGVEE IPDGTFEVDP
//
