ID A0A0F7PA02_9EURY Unreviewed; 278 AA.
AC A0A0F7PA02;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Hydroxyethylthiazole kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE EC=2.7.1.50 {ECO:0000256|HAMAP-Rule:MF_00228};
DE AltName: Full=4-methyl-5-beta-hydroxyethylthiazole kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE Short=TH kinase {ECO:0000256|HAMAP-Rule:MF_00228};
DE Short=Thz kinase {ECO:0000256|HAMAP-Rule:MF_00228};
GN Name=thiM {ECO:0000256|HAMAP-Rule:MF_00228,
GN ECO:0000313|EMBL:AKH97981.1};
GN ORFNames=HLASA_1489 {ECO:0000313|EMBL:ALG82375.1}, HLASF_1502
GN {ECO:0000313|EMBL:AKH97981.1};
OS Halanaeroarchaeum sulfurireducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halanaeroarchaeum.
OX NCBI_TaxID=1604004 {ECO:0000313|EMBL:AKH97981.1, ECO:0000313|Proteomes:UP000069906};
RN [1] {ECO:0000313|EMBL:AKH97981.1, ECO:0000313|Proteomes:UP000069906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HSR2 {ECO:0000313|EMBL:AKH97981.1,
RC ECO:0000313|Proteomes:UP000069906};
RX PubMed=25978546;
RA Sorokin D.Y., Kublanov I.V., Gavrilov S.N., Rojo D., Roman P.,
RA Golyshin P.N., Slepak V.Z., Smedile F., Ferrer M., Messina E., La Cono V.,
RA Yakimov M.M.;
RT "Elemental sulfur and acetate can support life of a novel strictly
RT anaerobic haloarchaeon.";
RL ISME J. 0:0-0(2015).
RN [2] {ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|Proteomes:UP000060390};
RA Messina E., Kublanov I.V., Toshchakov S., Arcadi E., La Spada G.,
RA La Cono V., Yakimov M.M.;
RT "Complete genome sequence of Halanaeroarchaeum sulfurireducens type strain
RT M27-SA2, a sulfate-reducer haloarchaeon from marine anoxic lake Medee.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ALG82375.1, ECO:0000313|Proteomes:UP000060390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M27-SA2 {ECO:0000313|EMBL:ALG82375.1,
RC ECO:0000313|Proteomes:UP000060390};
RX PubMed=27182430; DOI=10.1186/s40793-016-0155-9;
RA Messina E., Sorokin D.Y., Kublanov I.V., Toshchakov S., Lopatina A.,
RA Arcadi E., Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Complete genome sequence of 'Halanaeroarchaeum sulfurireducens' M27-SA2, a
RT sulfur-reducing and acetate-oxidizing haloarchaeon from the deep-sea
RT hypersaline anoxic lake Medee.";
RL Stand. Genomic Sci. 11:35-35(2016).
CC -!- FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-
CC methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000256|HAMAP-
CC Rule:MF_00228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-
CC phosphooxyethyl)-thiazole + ADP + H(+); Xref=Rhea:RHEA:24212,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17957, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58296, ChEBI:CHEBI:456216; EC=2.7.1.50;
CC Evidence={ECO:0000256|ARBA:ARBA00001771, ECO:0000256|HAMAP-
CC Rule:MF_00228};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_00228};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-
CC methylthiazole: step 1/1. {ECO:0000256|ARBA:ARBA00004868,
CC ECO:0000256|HAMAP-Rule:MF_00228}.
CC -!- SIMILARITY: Belongs to the Thz kinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00228}.
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DR EMBL; CP008874; AKH97981.1; -; Genomic_DNA.
DR EMBL; CP011564; ALG82375.1; -; Genomic_DNA.
DR RefSeq; WP_050048685.1; NZ_CP011564.1.
DR AlphaFoldDB; A0A0F7PA02; -.
DR STRING; 1604004.HLASA_1489; -.
DR GeneID; 26010832; -.
DR KEGG; hsf:HLASA_1489; -.
DR KEGG; hsu:HLASF_1502; -.
DR PATRIC; fig|1604004.4.peg.1567; -.
DR HOGENOM; CLU_019943_0_0_2; -.
DR OrthoDB; 214286at2157; -.
DR UniPathway; UPA00060; UER00139.
DR Proteomes; UP000060390; Chromosome.
DR Proteomes; UP000069906; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004417; F:hydroxyethylthiazole kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; 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-UniPathway.
DR CDD; cd01170; THZ_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00228; Thz_kinase; 1.
DR InterPro; IPR000417; Hyethyz_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF02110; HK; 1.
DR PIRSF; PIRSF000513; Thz_kinase; 1.
DR PRINTS; PR01099; HYETHTZKNASE.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00228};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00228, ECO:0000313|EMBL:AKH97981.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00228};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00228};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00228}; Reference proteome {ECO:0000313|Proteomes:UP000069906};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00228};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00228, ECO:0000313|EMBL:AKH97981.1}.
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00228"
SQ SEQUENCE 278 AA; 27570 MW; 7269183B334D1FD0 CRC64;
MSSPDDLGAP LAAVESGSPL VNALTNDVTV NEVANVILHW GGLPVMSDDE RELDEMIAAS
EATLLNMGTV SATGEATMMT AGQAAAAHDV PIVVDPVGAG ATTTRSRIAG RLATELSPDI
VKGNRGEIAA LAGDDADVRG VESVGEHDDI AETAMAFARQ TDAVVVATGT TDVVATDDAV
FEVGAGHSLM GDVVGTGCML GGTLAAFAGA VDDPVTAALS GTLALGLAGE AAAAGEYGEY
AGPASYEIAF LDAVAGLEPE TLSAASDRVS RVLVGDSG
//
