THIL_AQUAE
ID THIL_AQUAE Reviewed; 306 AA.
AC O67883;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE Short=TMP kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE Short=Thiamine-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128};
DE EC=2.7.4.16 {ECO:0000255|HAMAP-Rule:MF_02128};
GN Name=thiL; OrderedLocusNames=aq_2119;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH ATP; ADP; TMP; TPP
RP AND MAGNESIUM, FUNCTION, DISULFIDE BOND, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=18311927; DOI=10.1021/bi800041h;
RA McCulloch K.M., Kinsland C., Begley T.P., Ealick S.E.;
RT "Structural studies of thiamin monophosphate kinase in complex with
RT substrates and products.";
RL Biochemistry 47:3810-3821(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of thiamine monophosphate kinase (ThiL) from Aquifex
RT Aeolicus.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-
CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active
CC form of vitamin B1. {ECO:0000255|HAMAP-Rule:MF_02128,
CC ECO:0000305|PubMed:18311927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + thiamine phosphate = ADP + thiamine diphosphate;
CC Xref=Rhea:RHEA:15913, ChEBI:CHEBI:30616, ChEBI:CHEBI:37575,
CC ChEBI:CHEBI:58937, ChEBI:CHEBI:456216; EC=2.7.4.16;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02128};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC thiamine diphosphate from thiamine phosphate: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_02128}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18311927}.
CC -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a direct,
CC inline transfer of the gamma-phosphate of ATP to TMP rather than a
CC phosphorylated enzyme intermediate. {ECO:0000305|PubMed:18311927}.
CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_02128}.
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; AE000657; AAC07848.1; -; Genomic_DNA.
DR PIR; G70481; G70481.
DR RefSeq; NP_214452.1; NC_000918.1.
DR RefSeq; WP_010881388.1; NC_000918.1.
DR PDB; 1VQV; X-ray; 2.65 A; A/B=1-306.
DR PDB; 3C9R; X-ray; 2.30 A; A/B=1-306.
DR PDB; 3C9S; X-ray; 2.20 A; A/B=1-306.
DR PDB; 3C9T; X-ray; 2.60 A; A/B=1-306.
DR PDB; 3C9U; X-ray; 1.48 A; A/B=1-306.
DR PDBsum; 1VQV; -.
DR PDBsum; 3C9R; -.
DR PDBsum; 3C9S; -.
DR PDBsum; 3C9T; -.
DR PDBsum; 3C9U; -.
DR AlphaFoldDB; O67883; -.
DR SMR; O67883; -.
DR STRING; 224324.aq_2119; -.
DR EnsemblBacteria; AAC07848; AAC07848; aq_2119.
DR KEGG; aae:aq_2119; -.
DR PATRIC; fig|224324.8.peg.1635; -.
DR eggNOG; COG0611; Bacteria.
DR HOGENOM; CLU_046964_1_1_0; -.
DR InParanoid; O67883; -.
DR OMA; HFRRDWS; -.
DR OrthoDB; 1016556at2; -.
DR BRENDA; 2.7.4.16; 396.
DR UniPathway; UPA00060; UER00142.
DR EvolutionaryTrace; O67883; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02194; ThiL; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_02128; TMP_kinase; 1.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR006283; ThiL.
DR PANTHER; PTHR30270; PTHR30270; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR01379; thiL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Disulfide bond; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome;
KW Thiamine biosynthesis; Transferase.
FT CHAIN 1..306
FT /note="Thiamine-monophosphate kinase"
FT /id="PRO_0000415517"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 71
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 118..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18311927"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18311927"
FT DISULFID 34
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18311927"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 36..46
FT /evidence="ECO:0007829|PDB:3C9U"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 78..88
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 94..111
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 127..138
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 159..168
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 212..223
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3C9U"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3C9U"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:3C9U"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:3C9T"
FT STRAND 279..293
FT /evidence="ECO:0007829|PDB:3C9U"
SQ SEQUENCE 306 AA; 34413 MW; B5E5E63489D9BB32 CRC64;
MRLKELGEFG LIDLIKKTLE SKVIGDDTAP VEYCSKKLLL TTDVLNEGVH FLRSYIPEAV
GWKAISVNVS DVIANGGLPK WALISLNLPE DLEVSYVERF YIGVKRACEF YKCEVVGGNI
SKSEKIGISV FLVGETERFV GRDGARLGDS VFVSGTLGDS RAGLELLLME KEEYEPFELA
LIQRHLRPTA RIDYVKHIQK YANASMDISD GLVADANHLA QRSGVKIEIL SEKLPLSNEL
KMYCEKYGKN PIEYALFGGE DYQLLFTHPK ERWNPFLDMT EIGRVEEGEG VFVDGKKVEP
KGWKHF
