ID A0A075JNT9_9MICO Unreviewed; 272 AA.
AC A0A075JNT9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Hydroxymethylpyrimidine kinase {ECO:0000313|EMBL:AIF41808.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:AIF41808.1};
GN ORFNames=HX89_13775 {ECO:0000313|EMBL:AIF41808.1};
OS Dermacoccus nishinomiyaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Dermacoccus.
OX NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF41808.1, ECO:0000313|Proteomes:UP000027986};
RN [1] {ECO:0000313|EMBL:AIF41808.1, ECO:0000313|Proteomes:UP000027986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M25 {ECO:0000313|EMBL:AIF41808.1,
RC ECO:0000313|Proteomes:UP000027986};
RA Hong K.W., Chan K.G.;
RT "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000256|ARBA:ARBA00003848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-
CC amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP;
CC Xref=Rhea:RHEA:19893, ChEBI:CHEBI:30616, ChEBI:CHEBI:57841,
CC ChEBI:CHEBI:58354, ChEBI:CHEBI:456216; EC=2.7.4.7;
CC Evidence={ECO:0000256|ARBA:ARBA00000565};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-
CC methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+);
CC Xref=Rhea:RHEA:23096, ChEBI:CHEBI:15378, ChEBI:CHEBI:16892,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58354, ChEBI:CHEBI:456216;
CC EC=2.7.1.49; Evidence={ECO:0000256|ARBA:ARBA00000151};
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3. {ECO:0000256|ARBA:ARBA00004769}.
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DR EMBL; CP008889; AIF41808.1; -; Genomic_DNA.
DR RefSeq; WP_038569820.1; NZ_JAHHZR010000011.1.
DR AlphaFoldDB; A0A075JNT9; -.
DR GeneID; 41842100; -.
DR KEGG; dni:HX89_13775; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_1_11; -.
DR OrthoDB; 34166at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000027986; Chromosome.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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; cd01169; HMPP_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR PANTHER; PTHR20858:SF17; HYDROXYMETHYLPYRIMIDINE_PHOSPHOMETHYLPYRIMIDINE KINASE THI20-RELATED; 1.
DR PANTHER; PTHR20858; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AIF41808.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027986};
KW Transferase {ECO:0000313|EMBL:AIF41808.1}.
FT DOMAIN 13..266
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 272 AA; 28262 MW; 5C494737B890CE64 CRC64;
MSTPNVLTIA GTDPSGGAGI MADLKAFGAL RTHGCAVVTA VVAQNTRGVA AVTQMTSQQV
RTQLENLVDD VRIDALKIGM LGSAAVIETV ADVLADHPAL RGVPRVLDPV MVASSGDRLI
DEDAVTALRE RLVPEVDVIT PNLAEAAVLL DLDDAPREAS DDVARALVAL GSGVLLKGGH
GGGAKSDDVL LVPAESDEPA RLSAPRIDTR NTHGTGCTLS AAMTALRPQR DSWAQATREA
KEYVTEALAA SGDLDVGRGD GHGPVHHFHA WW
//
