ID A0A2L0EHC5_SORCE Unreviewed; 340 AA.
AC A0A2L0EHC5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN ORFNames=SOCE26_000660 {ECO:0000313|EMBL:AUX38688.1};
OS Sorangium cellulosum (Polyangium cellulosum).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=56 {ECO:0000313|EMBL:AUX38688.1, ECO:0000313|Proteomes:UP000238348};
RN [1] {ECO:0000313|EMBL:AUX38688.1, ECO:0000313|Proteomes:UP000238348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce26 {ECO:0000313|EMBL:AUX38688.1,
RC ECO:0000313|Proteomes:UP000238348};
RA Zaburannyi N., Bunk B., Overmann J., Mueller R.;
RT "Sorangium comparison.";
RL Submitted (SEP-2015) 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; CP012673; AUX38688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0EHC5; -.
DR OrthoDB; 174578at2; -.
DR Proteomes; UP000238348; Chromosome.
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 Signal {ECO:0000256|SAM:SignalP};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..340
FT /note="Thiamine pyrimidine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014636329"
FT DOMAIN 60..264
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 340 AA; 36565 MW; 8EA659093BFC6C0C CRC64;
MNARVFGFLF WFGLVFAAFG CSREQAPSAG GTAGSAPAAA GSAAAAPAKV KLVLNWVPEP
EFGGFYAARE IGAYKRNGLE VEILGGGAGV PVLQMVATGK AEYGISNADE IITAVSRGAD
IVALFTIYQT FPQGIMAHPS RGAKSMADVL SSGTLAIEPG VPYAAFLKKK YGFDKVKIVP
YDGGVARFIA EKDFAQQCFV TAEPVAARRK GVEPTVFLVA DEGFNPYAGV VIARKALWKE
HPEQVRAFVR ASREGWRAYL DDPTPANAVM AKLNTGMDAD TFKTAAELQE KFVETEETKK
KPNGLGQMTR ERWETMGKQL VELGHIERAP AVDDYLVTIE
//
