(data stored in SCRATCH zone)

SWISSPROT: D5E9K2_METMS

ID   D5E9K2_METMS            Unreviewed;       294 AA.
AC   D5E9K2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 48.
DE   RecName: Full=Thiamine-monophosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE            Short=TMP kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE            Short=Thiamine-phosphate kinase {ECO:0000256|HAMAP-Rule:MF_02128};
DE            EC=2.7.4.16 {ECO:0000256|HAMAP-Rule:MF_02128};
GN   Name=thiL {ECO:0000256|HAMAP-Rule:MF_02128};
GN   OrderedLocusNames=Mmah_0321 {ECO:0000313|EMBL:ADE35853.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35853.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35853.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_02128}.
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:0000256|HAMAP-Rule:MF_02128};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis;
CC       thiamine diphosphate from thiamine phosphate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_02128}.
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:0000256|HAMAP-Rule:MF_02128}.
CC   -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_02128}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|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; CP001994; ADE35853.1; -; Genomic_DNA.
DR   EnsemblBacteria; ADE35853; ADE35853; Mmah_0321.
DR   KEGG; mmh:Mmah_0321; -.
DR   eggNOG; arCOG00638; Archaea.
DR   eggNOG; COG0611; LUCA.
DR   HOGENOM; HOG000228430; -.
DR   KO; K00946; -.
DR   OMA; HFRRDWS; -.
DR   BioCyc; MMAH547558:G1GHT-317-MONOMER; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000001059; 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: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   3: Inferred from homology;
DR   PRODOM; D5E9K2.
DR   SWISS-2DPAGE; D5E9K2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:ADE35853.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:ADE35853.1}.
FT   DOMAIN          12..110
FT                   /note="AIRS"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          122..263
FT                   /note="AIRS_C"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   NP_BIND         92..93
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           15
FT                   /note="Magnesium 4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           16
FT                   /note="Magnesium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           17
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           17
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           45
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           45
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           45
FT                   /note="Magnesium 4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           93
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           181
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   METAL           184
FT                   /note="Magnesium 5"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         24
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         118
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         183
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT   BINDING         285
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
SQ   SEQUENCE   294 AA;  31248 MW;  060764E2ACCC8AC2 CRC64;
     MTAVLEFGGE YLVVTTDMLH QKTDFPDTMT PWQIGWMAAA VNFSDIAAMG GQPLGLLAAV
     GYPQNMSLED AGEIARGMRD CAEFCGTSVI GGDVDSHEEL TVTGTAMGRV SKEELLTRKG
     AKPGDLLCVT ATLGGAGAAL EAYLKNMNVD DDFMKPLLEP VPRIAEGRKL AKSGAVTSAM
     DTSDGLALSL YDLASVNKVG FVLKEESLPI DKRVFEIATS KKEALEMALY SGGDFELLVT
     VSKDKFKALQ AESYLTVVGE VVDIDGAISL IGKDGANFAI DRKGYLHMGT SDQI
//

If you have problems or comments...

PBIL Back to PBIL home page