ID A6TVU4_ALKMQ Unreviewed; 196 AA.
AC A6TVU4;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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 OrderedLocusNames=Amet_4232 {ECO:0000313|EMBL:ABR50312.1};
OS Alkaliphilus metalliredigens (strain QYMF).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR50312.1, ECO:0000313|Proteomes:UP000001572};
RN [1] {ECO:0000313|Proteomes:UP000001572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572};
RX PubMed=27811105; DOI=10.1128/genomeA.01226-16;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina Del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F.,
RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J.,
RA Richardson P., Fields M.W.;
RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an
RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated
RT leachate ponds.";
RL Genome Announc. 4:0-0(2016).
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}.
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DR EMBL; CP000724; ABR50312.1; -; Genomic_DNA.
DR RefSeq; WP_012065260.1; NC_009633.1.
DR AlphaFoldDB; A6TVU4; -.
DR STRING; 293826.Amet_4232; -.
DR KEGG; amt:Amet_4232; -.
DR eggNOG; COG0352; Bacteria.
DR HOGENOM; CLU_018272_3_4_9; -.
DR OrthoDB; 9815348at2; -.
DR UniPathway; UPA00060; UER00141.
DR Proteomes; UP000001572; Chromosome.
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:UP000001572};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977,
KW ECO:0000256|RuleBase:RU003826};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003826}.
FT DOMAIN 2..178
FT /note="Thiamine phosphate synthase/TenI"
FT /evidence="ECO:0000259|Pfam:PF02581"
SQ SEQUENCE 196 AA; 21345 MW; 037CC1B29DEEA0B4 CRC64;
MLYLVTNRRM IEDHNFLSVI KGATNGGVDA IILREKDLSY KELLGLAKDI QGVVHGTNTR
LIINNSLEVA NAVGAHGYHT GFQQFIEKRL HFQGGVGVSV HSIEEGIEAE NQGASYLLVG
HIFETNSKKN LPPKGITFIE GFKKNIKIPI VAIGGINAGN IQQLCRVKVD GVAVMSEIMM
ATDPHATTAK LKNLMK
//
