ID A0A037ZF68_9RHOB Unreviewed; 198 AA.
AC A0A037ZF68;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Thiamine-phosphate synthase {ECO:0000256|RuleBase:RU003826};
DE EC=2.5.1.3 {ECO:0000256|RuleBase:RU003826};
DE AltName: Full=Thiamine-phosphate pyrophosphorylase {ECO:0000256|RuleBase:RU003826};
GN ORFNames=ACMU_18710 {ECO:0000313|EMBL:KAJ54258.1};
OS Actibacterium mucosum KCTC 23349.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Actibacterium.
OX NCBI_TaxID=1454373 {ECO:0000313|EMBL:KAJ54258.1, ECO:0000313|Proteomes:UP000026249};
RN [1] {ECO:0000313|EMBL:KAJ54258.1, ECO:0000313|Proteomes:UP000026249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 23349 {ECO:0000313|EMBL:KAJ54258.1,
RC ECO:0000313|Proteomes:UP000026249};
RA Arahal D.R., Shao Z., Lai Q., Pujalte M.J.;
RT "Draft Genome Sequence of Actibacterium mucosum KCTC 23349, a Marine
RT Alphaproteobacterium with Complex Ionic Requirements Isolated from
RT Mediterranean Seawater at Malvarrosa Beach, Valencia, Spain.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate
CC + thiamine phosphate; Xref=Rhea:RHEA:47848, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:33019, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:57841, ChEBI:CHEBI:62890; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00000876,
CC ECO:0000256|RuleBase:RU003826};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl
CC phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2
CC H(+) = CO2 + diphosphate + thiamine phosphate; Xref=Rhea:RHEA:47844,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37575, ChEBI:CHEBI:57841, ChEBI:CHEBI:62899; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001829,
CC ECO:0000256|RuleBase:RU003826};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 4-methyl-
CC 5-(2-phosphooxyethyl)-thiazole + H(+) = diphosphate + thiamine
CC phosphate; Xref=Rhea:RHEA:22328, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37575, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58296; EC=2.5.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001159,
CC ECO:0000256|RuleBase:RU003826};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine
CC and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005165}.
CC -!- SIMILARITY: Belongs to the thiamine-phosphate synthase family.
CC {ECO:0000256|RuleBase:RU003826}.
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:KAJ54258.1}.
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DR EMBL; JFKE01000009; KAJ54258.1; -; Genomic_DNA.
DR RefSeq; WP_035261895.1; NZ_JFKE01000009.1.
DR AlphaFoldDB; A0A037ZF68; -.
DR STRING; 1454373.ACMU_18710; -.
DR OrthoDB; 9794842at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000026249; Unassembled WGS sequence.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR InterPro; IPR034291; TMP_synthase.
DR NCBIfam; TIGR00693; thiE; 1.
DR PANTHER; PTHR20857:SF15; THIAMINE BIOSYNTHETIC BIFUNCTIONAL ENZYME; 1.
DR PANTHER; PTHR20857; THIAMINE-PHOSPHATE PYROPHOSPHORYLASE; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Reference proteome {ECO:0000313|Proteomes:UP000026249};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977,
KW ECO:0000256|RuleBase:RU003826};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003826}.
FT DOMAIN 12..180
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
SQ SEQUENCE 198 AA; 21834 MW; CBC488C43031FA49 CRC64;
MTLDRFYPIF DDVRWLERML PLGVKLVQLR IKEADDATLR DQITRAKALC DDAGAVLVVN
DYWQMAIELG CDWVHLGQED LDEADVSAIR AAGLKLGLST HDPSELARAM SHAPDYVALG
PVYPTILKKM KWHQQGLERV TVWKGLVGDT PLVAIGGMSV ERAPGAFAAG ADIVSAVTDI
TLNDDPEARV RAWLEVTR
//
