(data stored in ACNUC7421 zone)

SWISSPROT: D4YXM9_SPHJU

ID   D4YXM9_SPHJU            Unreviewed;       304 AA.
AC   D4YXM9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 45.
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   ECO:0000313|EMBL:BAI95111.1};
GN   OrderedLocusNames=SJA_C1-02770 {ECO:0000313|EMBL:BAI95111.1};
OS   Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS   / NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95111.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95111.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC   {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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; AP010803; BAI95111.1; -; Genomic_DNA.
DR   RefSeq; WP_013038911.1; NC_014006.1.
DR   STRING; 452662.SJA_C1-02770; -.
DR   EnsemblBacteria; BAI95111; BAI95111; SJA_C1-02770.
DR   GeneID; 29271980; -.
DR   KEGG; sjp:SJA_C1-02770; -.
DR   eggNOG; ENOG4105CG2; Bacteria.
DR   eggNOG; COG0611; LUCA.
DR   HOGENOM; HOG000228429; -.
DR   KO; K00946; -.
DR   OMA; HFRRDWS; -.
DR   UniPathway; UPA00060; UER00142.
DR   Proteomes; UP000007753; Chromosome 1.
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; D4YXM9.
DR   SWISS-2DPAGE; D4YXM9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:BAI95111.1};
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:UP000007753};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02128,
KW   ECO:0000313|EMBL:BAI95111.1}.
FT   DOMAIN       25    135       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      147    234       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   NP_BIND     115    116       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        26     26       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        26     26       Magnesium 4; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        40     40       Magnesium 4. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        41     41       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   METAL        42     42       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        42     42       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        70     70       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        70     70       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL        70     70       Magnesium 4. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       116    116       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       204    204       Magnesium 3. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   METAL       207    207       Magnesium 5. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING      49     49       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING     143    143       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   BINDING     206    206       ATP. {ECO:0000256|HAMAP-Rule:MF_02128}.
FT   BINDING     254    254       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
FT   BINDING     301    301       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_02128}.
SQ   SEQUENCE   304 AA;  31426 MW;  C48D399EEC1C5323 CRC64;
     MSAESRFLTL LRLLANDPAA QGLRDDVAVL EVGGARLILT SDTMVEGVHH LPADPPADIG
     WKLAAVNLSD LAAKGAKPLG CLLNYALSGD ESWDAAFLEG LGEALARHAM PLLGGDTVQM
     PRGAPRSYSL TALGEATGPV PLRGGAKAGD RLYLTGPVGD AGIGLELLQT MPRASGPLVD
     AYRRPRPRLA EGALLAPHVH AMMDVSDGLL IDAARMAEAS GLAVTIDHIP LSPALEATRG
     ASNAVQIAAA RAGDDYELLF ALPAAVKPPV RAIPVGRFAK GGGLTLKIDG VAIPLPDRLG
     WEHG
//

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