ID F5LEA0_9BACL Unreviewed; 305 AA.
AC F5LEA0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00019161};
DE EC=2.7.1.49 {ECO:0000256|ARBA:ARBA00012135};
DE EC=2.7.4.7 {ECO:0000256|ARBA:ARBA00012963};
DE AltName: Full=Hydroxymethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00042102};
DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase {ECO:0000256|ARBA:ARBA00043176};
GN Name=thiD {ECO:0000313|EMBL:EGL19312.1};
GN ORFNames=HMPREF9413_2718 {ECO:0000313|EMBL:EGL19312.1};
OS Paenibacillus sp. HGF7.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL19312.1, ECO:0000313|Proteomes:UP000003445};
RN [1] {ECO:0000313|EMBL:EGL19312.1, ECO:0000313|Proteomes:UP000003445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF7 {ECO:0000313|EMBL:EGL19312.1,
RC ECO:0000313|Proteomes:UP000003445};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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 2/3. {ECO:0000256|ARBA:ARBA00037917}.
CC -!- SIMILARITY: Belongs to the ThiD family.
CC {ECO:0000256|ARBA:ARBA00009879}.
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:EGL19312.1}.
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DR EMBL; AFDH01000026; EGL19312.1; -; Genomic_DNA.
DR RefSeq; WP_009672288.1; NZ_AFDH01000026.1.
DR AlphaFoldDB; F5LEA0; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000003445; Unassembled WGS sequence.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:RHEA.
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:InterPro.
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 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EGL19312.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003445};
KW Transferase {ECO:0000313|EMBL:EGL19312.1}.
FT DOMAIN 31..276
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 305 AA; 31948 MW; 03DA9B0828B2BBE3 CRC64;
MNMSLNKQQY PPEPRRQAPL VPAAATIAGS DSGGGAGIQA DLKTFQELGV FGASALTAVT
AQNTLGVHGV HPIPPSMVAA QIDAVAGDIG PAAWKTGMLF SAEIIEAVAD RATFYKWSRL
VVDPVMIAKG GASLLQEDAV QALRSLLLPL AQVVTPNIPE AEALTGMRIA TMADRKEAAR
RIHAWGVKYV VLKGGHGGNR AQSLDLLYDG RVFTEFAAPW VETRHTHGTG CTFAAALTAG
LASGLPMDEA VLLAKRFIQA ALENPLNLGA GHGPTNHWGY NRPGTAGAFF KTAPAAAGES
EGWLR
//
