ID A0A087BRD7_9BIFI Unreviewed; 364 AA.
AC A0A087BRD7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN ORFNames=BMIN_1022 {ECO:0000313|EMBL:KFI73587.1};
OS Bifidobacterium minimum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI73587.1, ECO:0000313|Proteomes:UP000029014};
RN [1] {ECO:0000313|EMBL:KFI73587.1, ECO:0000313|Proteomes:UP000029014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI73587.1,
RC ECO:0000313|Proteomes:UP000029014};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI73587.1}.
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DR EMBL; JGZD01000006; KFI73587.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BRD7; -.
DR STRING; 1693.BMIN_1022; -.
DR eggNOG; COG0715; Bacteria.
DR Proteomes; UP000029014; 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.
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:UP000029014};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..364
FT /note="Thiamine pyrimidine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039464042"
FT DOMAIN 60..275
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
FT REGION 340..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 364 AA; 38379 MW; 97853AD72301907C CRC64;
MLGNSSVRAF ATRTTRLFRM AAATTSAIAL LAATAACGSA ASNSSDGTPT VTFMLDWTPN
TNHVGLYVAQ KLGYFKDAGI NVTILPTAQA GAETSVENGV ANVGFTTLSN VAAFNAQGAD
LKFVFDLTQK PVARWCALAS RTDIKTPKDL SGKTFVSFGS AEQSAVVKQM IKYAGGTGTF
STATTGTNTF ETLTSGKGDF GGFYVTWENV QSELNGPKLH CFVASDWGVP GNPDQLGYAV
KASWAKDASH AAALRKFIHA AQRGYDYALK NPDKAADILV DQTPTAQLDS KLARRSMEEI
SSGHYWTTTD PTAVPGTTDL KQAQAYLDFQ FAAGTYTNAD GKTAKTAPQA SELSTGKYLS
ATNA
//
