ID A0A1I0VC80_9CELL Unreviewed; 387 AA.
AC A0A1I0VC80;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Thiamine pyrimidine synthase {ECO:0000256|ARBA:ARBA00033171};
GN ORFNames=SAMN05421867_101311 {ECO:0000313|EMBL:SFA73941.1};
OS Cellulomonas marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=988821 {ECO:0000313|EMBL:SFA73941.1, ECO:0000313|Proteomes:UP000199012};
RN [1] {ECO:0000313|EMBL:SFA73941.1, ECO:0000313|Proteomes:UP000199012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6945 {ECO:0000313|EMBL:SFA73941.1,
RC ECO:0000313|Proteomes:UP000199012};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOKA01000001; SFA73941.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0VC80; -.
DR STRING; 988821.SAMN05421867_101311; -.
DR OrthoDB; 174578at2; -.
DR Proteomes; UP000199012; 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:UP000199012};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..387
FT /note="Thiamine pyrimidine synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038492642"
FT DOMAIN 58..280
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
SQ SEQUENCE 387 AA; 40907 MW; 44B7FFBAC843C041 CRC64;
MTRTPRAALR LTAAGLGLAL ALTACSSGGG DAEPAASGSG GEGGLTPVKL QLQWFTQAQF
AGYYAALEQG FYEDAGLDVE IVEGGVDIVP QTELANGAVD YAIAWVPKAL ASREQGAGIT
DVAQIFQRSG TLQVSFADAG IDSAADLAGK KVGNWGFGNE FELFAGMTAA GLDPATDVTL
VQQQFDMNAL LSGEIDAAQA MTYNEYAQVL EAENPETGEL YRPEDFSVVD WNEEGTAMLQ
DAIWANSERL ASDEEYQETT VAFIKASIQG WVFARDEAEA ARDLVVAAGS QLGNSHQLWQ
VNEVNKLIWP SPDGIGTIDE DLWDQTVEVA LTAKNDQGAT VITAEPDAEA YTNEYVEQAL
AELEAEGVDV TGEGFQPLTV TLEAGGA
//
