ID A0A238W1S5_9ACTN Unreviewed; 326 AA.
AC A0A238W1S5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN ORFNames=SAMN06264365_10287 {ECO:0000313|EMBL:SNR40476.1};
OS Actinoplanes regularis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=52697 {ECO:0000313|EMBL:SNR40476.1, ECO:0000313|Proteomes:UP000198415};
RN [1] {ECO:0000313|EMBL:SNR40476.1, ECO:0000313|Proteomes:UP000198415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43151 {ECO:0000313|EMBL:SNR40476.1,
RC ECO:0000313|Proteomes:UP000198415};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZNR01000002; SNR40476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238W1S5; -.
DR OrthoDB; 174578at2; -.
DR Proteomes; UP000198415; 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-KW.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000198415};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..326
FT /note="Thiamine pyrimidine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038490498"
FT DOMAIN 48..257
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 326 AA; 33921 MW; 014BE8E3FD338B80 CRC64;
MRRLAVACSA FLAVALLLAG CGEEKKAPGD KVTYLTAFGA VGRDAFAWVA QEKGYFRDAG
LDVTIQLGAA TGENLKVLAA GRAQFASLDL TGMWILAGKG EYPDVRAIAA IHQQTLVSIV
SLEGAGVTQP KDLEGRQVGA ATGSVNQLLF PAYAGLAGVD PAKVKWVNAP PAQLPALLAS
GRVNALSTFL IGAKGLSKAA GGKPTVVLPY STYLPELFGN GLVAPLAITR DQPDVARRFR
DAALKGLQYT LEHPEEAAQI MKKAQPAADV TAAVGEITLM KPYVKPSGVI DRQRVAAAIA
TLEKNKLIPP GLTPDSVVDF ALAPAS
//
