ID K8GM66_9CYAN Unreviewed; 328 AA.
AC K8GM66;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, 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 ORFNames=OsccyDRAFT_0336 {ECO:0000313|EMBL:EKQ70072.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ70072.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ70072.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ70072.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ70072.1}.
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DR EMBL; AJUB01000005; EKQ70072.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GM66; -.
DR STRING; 864702.OsccyDRAFT_0336; -.
DR PATRIC; fig|864702.5.peg.363; -.
DR eggNOG; COG0611; Bacteria.
DR HOGENOM; CLU_046964_3_0_3; -.
DR OrthoDB; 9802811at2; -.
DR UniPathway; UPA00060; UER00142.
DR Proteomes; UP000001332; 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; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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-like.
DR NCBIfam; TIGR01379; thiL; 1.
DR PANTHER; PTHR30270; THIAMINE-MONOPHOSPHATE KINASE; 1.
DR PANTHER; PTHR30270:SF0; THIAMINE-MONOPHOSPHATE KINASE; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02128};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02128, ECO:0000313|EMBL:EKQ70072.1};
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:UP000001332};
KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02128};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02128}.
FT DOMAIN 25..137
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 197..303
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 27
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 120..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="5"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
FT BINDING 324
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02128"
SQ SEQUENCE 328 AA; 35565 MW; D93874989881E6B1 CRC64;
MNVREIGEQE LLQRLQVFCP AEMIGDDAAV LTPQPGLSLV VTTDMLVDNV HFSDRTTTPE
DAGWRAAAAN LSDLAAMGAS PIGLTVGLGL PGDTPIEWVE RVYHGLVECL QPYNTMIMGG
DVVRSPVTTI AITAFGQASP QRLIRRANAK PDQAILVTGW HGASRAGLEL LLNPEIPQSL
SFQEQTFFKR AHQRPIPRLD VLPLLEQTQE IMIAGMDSSD GLADAVLQIC RASGVGARLE
RSQLPIPPGL VNWVGEQTAV QWTLYGGEDF ELVLCLPHIQ AERLCKQLGK GATIVGQTTV
EPDVLVVDSS GDNPCDRLTF DQGFQHFL
//
