ID Q1MQ91_LAWIP Unreviewed; 277 AA.
AC Q1MQ91;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:CAJ54836.1};
GN Name=thiD {ECO:0000313|EMBL:CAJ54836.1};
GN OrderedLocusNames=LI0782 {ECO:0000313|EMBL:CAJ54836.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54836.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54836.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54836.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; AM180252; CAJ54836.1; -; Genomic_DNA.
DR RefSeq; WP_011526865.1; NC_008011.1.
DR AlphaFoldDB; Q1MQ91; -.
DR STRING; 363253.LI0782; -.
DR KEGG; lip:LI0782; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_7; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000002430; Chromosome.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
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:CAJ54836.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002430};
KW Transferase {ECO:0000313|EMBL:CAJ54836.1}.
FT DOMAIN 19..267
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 277 AA; 29803 MW; 49B639A5297F0C9B CRC64;
MGKSSPSNPP CILTIAGSDS GGGAGIQADL KTIAILGGFG LSVITALTAQ NGLGVTGIHT
PDPSFIELQL NTIYKGFFVN VLKTGMLFSV PIIEIVKNII KKQQTLAVID PVCVSQSGYQ
LLEHTAIDAL RTHILPLAML VTPNKPEAEL LTEMQIESEK DIYIAGKRLI DMGAKAVLIK
GGHFYKNNLV TNYVDWYIEK NSTNPIPLSQ PAIKTKNNHG TGCTLSAAIA TYIGLGLELK
KAILQAQTYL NYCLKFSYTP GKGIGPPNHT AWLNRKL
//
