ID A0A0U3KEP7_9BURK Unreviewed; 362 AA.
AC A0A0U3KEP7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN ORFNames=Hrubri_4187 {ECO:0000313|EMBL:ALU91334.1};
OS Herbaspirillum rubrisubalbicans M1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU91334.1, ECO:0000313|Proteomes:UP000069903};
RN [1] {ECO:0000313|EMBL:ALU91334.1, ECO:0000313|Proteomes:UP000069903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ALU91334.1,
RC ECO:0000313|Proteomes:UP000069903};
RA Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL Submitted (DEC-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; CP013737; ALU91334.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3KEP7; -.
DR STRING; 1078773.Hrubri_4187; -.
DR KEGG; hrb:Hrubri_4187; -.
DR Proteomes; UP000069903; 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.
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 62..277
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 362 AA; 39411 MW; B994D3B7434D69EB CRC64;
MLLQRWDLAF QTNKEGKSTV YSSKFFKIGM SLLLSASCSL AVAQETKIKF QLDWRFEGPA
ALFLVAKSKG YFAQEKLDVT IDAGNGSGNA VNRVASGTYD MGFADMAALM EFTANNPDAP
GKPVAVMMVY NDTPAAVFSL KKSGIKKPAD LVGKKLGAPV FDAGRRAYPI FAKANGLDAS
KAQWTSMDPP LRETMLARGD VDAITGFYFT SLLNLNARGI KDEDINVMMY PDYGVRLYGN
TIIASEAMIK NKPEAIKGFL RAFAKASRDV MANPEAAIKV LKERDGLIDE KLELRRLKLA
IASAIATPHA KAEGYGQVNS PRLTLMASQV SDAYGTKTRV NADKIWNGSF LPSKAELDVF
PK
//
