ID F6BD11_METIK Unreviewed; 423 AA.
AC F6BD11;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 28-JAN-2026, entry version 60.
DE RecName: Full=Bifunctional thiamine biosynthesis protein ThiDN {ECO:0000256|ARBA:ARBA00067160};
DE EC=2.5.1.3 {ECO:0000256|ARBA:ARBA00012830};
DE EC=2.7.1.49 {ECO:0000256|ARBA:ARBA00012135};
DE EC=2.7.4.7 {ECO:0000256|ARBA:ARBA00012963};
GN OrderedLocusNames=Metig_0827 {ECO:0000313|EMBL:AEF96372.1};
OS Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5).
OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC Methanococci; Methanococcales; Methanocaldococcaceae; Methanotorris.
OX NCBI_TaxID=880724 {ECO:0000313|Proteomes:UP000009227};
RN [1] {ECO:0000313|EMBL:AEF96372.1, ECO:0000313|Proteomes:UP000009227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5666 / JCM 11834 / Kol 5
RC {ECO:0000313|Proteomes:UP000009227};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Chertkov O., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Sieprawska-Lupa M.,
RA Whitman W., Woyke T.;
RT "Complete sequence of Methanotorris igneus Kol 5.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000256|ARBA:ARBA00003848}.
CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole
CC monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine
CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
CC {ECO:0000256|ARBA:ARBA00059241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-
CC methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = thiamine phosphate
CC + CO2 + diphosphate; 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:ARBA00047851};
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(+) = thiamine phosphate + CO2 + diphosphate; 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:ARBA00047883};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000565};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methyl-5-(2-phosphooxyethyl)-thiazole + 4-amino-2-methyl-5-
CC (diphosphooxymethyl)pyrimidine + H(+) = thiamine phosphate +
CC diphosphate; 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:ARBA00047334};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole. {ECO:0000256|ARBA:ARBA00060674}.
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: In the C-terminal section; belongs to the ThiN family.
CC {ECO:0000256|ARBA:ARBA00060834}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ThiD family.
CC {ECO:0000256|ARBA:ARBA00060992}.
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DR EMBL; CP002737; AEF96372.1; -; Genomic_DNA.
DR RefSeq; WP_013798974.1; NC_015562.1.
DR AlphaFoldDB; F6BD11; -.
DR STRING; 880724.Metig_0827; -.
DR GeneID; 10643668; -.
DR KEGG; mig:Metig_0827; -.
DR HOGENOM; CLU_035788_0_0_2; -.
DR OrthoDB; 43786at2157; -.
DR Proteomes; UP000009227; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01169; HMPP_kinase; 1.
DR FunFam; 3.40.225.10:FF:000015; Phosphomethylpyrimidine kinase (Hmp-phosphate kinase); 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR019293; ThiN.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF10120; ThiN; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEF96372.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000009227};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEF96372.1}.
FT DOMAIN 13..238
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT DOMAIN 254..414
FT /note="Thiamine-phosphate synthase ThiN"
FT /evidence="ECO:0000259|Pfam:PF10120"
SQ SEQUENCE 423 AA; 47396 MW; 6F28BA5BE96F9261 CRC64;
MEKHNILIIG GYDPTGGAGV IADAKTAKVL GVNPLTITTS IIPQNNKAVY NKVDIPKKVI
KEQLDAIFED FDVSIVKTGV LNEDAINLIL KYKKDYDFKI VCDPVLKSTT NYEFVDENLL
EKHVDLFNEC YLITPNEEEF NTIINFIEKN NLWKKFDKNP YVLVTGTNDK LITLKDKNVI
ETIKGKKIDK EVHGTGCVFS SAIASFLCRG EELIDAIKKA KDIVLASVVY ATKTKYGYNS
NPTYINKEKV IKNLSYALYL LKKINFSLIP EVGSNIAESL LLPNSFKDVA ALTGRIIKNK
LGGFYIVGDI EFGASEHIAK IILAAKNYDP QIRACMNIRY DEDLIDVLSE KFSISSFDRK
LEPPNVSTME WGTKYACEKF GGVPDIIYDK GGDGKEPMIR VLGVDAIDVV KKVAEIQRIY
DRM
//
