(data stored in SCRATCH zone)

SWISSPROT: D6XY11_BACIE

ID   D6XY11_BACIE            Unreviewed;       332 AA.
AC   D6XY11;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
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=Bsel_0548 {ECO:0000313|EMBL:ADH98084.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98084.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH98084.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-
CC       monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the
CC       active 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
CC       direct, inline transfer of the gamma-phosphate of ATP to TMP
CC       rather than a phosphorylated enzyme intermediate.
CC       {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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_02128}.
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DR   EMBL; CP001791; ADH98084.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0548; -.
DR   EnsemblBacteria; ADH98084; ADH98084; Bsel_0548.
DR   KEGG; bse:Bsel_0548; -.
DR   eggNOG; ENOG4105CG2; Bacteria.
DR   eggNOG; COG0611; LUCA.
DR   HOGENOM; HOG000228428; -.
DR   KO; K00946; -.
DR   OMA; HFRRDWS; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000000271; 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; D6XY11.
DR   SWISS-2DPAGE; D6XY11.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:ADH98084.1};
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:UP000000271};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02128,
KW   ECO:0000313|EMBL:ADH98084.1}.
FT   DOMAIN       27    141       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      153    306       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   NP_BIND     122    123       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        28     28       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        28     28       Magnesium 4; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        45     45       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        45     45       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        74     74       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        74     74       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        74     74       Magnesium 4. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       123    123       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       219    219       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       222    222       Magnesium 5. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING      52     52       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING     105    105       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   BINDING     149    149       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   BINDING     221    221       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   BINDING     269    269       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING     325    325       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
SQ   SEQUENCE   332 AA;  36166 MW;  FA62DA98528846A7 CRC64;
     MDKEFAWIAS IRQKRMLSED VELGIGDDAA IVRVPDGYDQ VLAVDTMVED VHFSRATMAP
     EDIGYKALAV NISDLAAMGA VPKQYLVSLA VPKQGWPDEE TRRIYAGLEE AAALYGMDLI
     GGDTVSTADK LVISVTVTGI VETSVRLLRA NARPGDVIAV TGPLGASLAG LDLLLDQTNG
     VPVPEMDQDQ LIRSHQRPVP QVKAGRLFAE LGIRAALNDI SDGISREAKE IAEASGVRMV
     LDWKRIPKPD ILALFDEEKQ KDWVLHGGEE FQLVCVFSGK HWRDVCLLAE QHGITISPVG
     MVEAGEPAVI LIDGQESETL TKSGYDHFRD RE
//

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