ID Q0AS92_MARMM Unreviewed; 269 AA.
AC Q0AS92;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ABI64845.1};
GN OrderedLocusNames=Mmar10_0552 {ECO:0000313|EMBL:ABI64845.1};
OS Maricaulis maris (strain MCS10).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC Maricaulis.
OX NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI64845.1, ECO:0000313|Proteomes:UP000001964};
RN [1] {ECO:0000313|EMBL:ABI64845.1, ECO:0000313|Proteomes:UP000001964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCS10 {ECO:0000313|EMBL:ABI64845.1,
RC ECO:0000313|Proteomes:UP000001964};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA Stephens C., Richardson P.;
RT "Complete sequence of Maricaulis maris MCS10.";
RL Submitted (AUG-2006) 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; CP000449; ABI64845.1; -; Genomic_DNA.
DR RefSeq; WP_011642492.1; NC_008347.1.
DR AlphaFoldDB; Q0AS92; -.
DR STRING; 394221.Mmar10_0552; -.
DR KEGG; mmr:Mmar10_0552; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_3_5; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000001964; 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:ABI64845.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001964};
KW Transferase {ECO:0000313|EMBL:ABI64845.1}.
FT DOMAIN 17..262
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 269 AA; 27355 MW; 7F8523E4221A4A8B CRC64;
MDDTEPKGRV LIIAGSDSGG GAGIQADIKA VTAMGGFAAT AITAITVQNT LGVSAIHPVP
LDIIKGQIDA VLSDIGADVI KTGMLGTCEI VTLVADCLAA CEVPIPLVLD PVMVATSGDL
LVDEGAQAAI RDRLLPMATL VTPNIPEAEK LTGLAVTDIA GQLEAANRLI EMGARAALVK
GGHLKGQAVA DVLVSTRGME LFDRPRLPGR NTHGTGCTLA SAIAGLLADG APLHDAVRRA
GDYLHEAIAR APGFGAGHGP VNHAWVTRP
//
