ID F0RQ01_DEIPM Unreviewed; 247 AA.
AC F0RQ01;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ADY27203.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:ADY27203.1};
GN OrderedLocusNames=Deipr_2072 {ECO:0000313|EMBL:ADY27203.1};
OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC
OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OG Plasmid pDEIPR01 {ECO:0000313|EMBL:ADY27203.1,
OG ECO:0000313|Proteomes:UP000007718}.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY27203.1, ECO:0000313|Proteomes:UP000007718};
RN [1] {ECO:0000313|EMBL:ADY27203.1, ECO:0000313|Proteomes:UP000007718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RC PLASMID=Plasmid pDEIPR01 {ECO:0000313|Proteomes:UP000007718};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete sequence of plasmid1 of Deinococcus proteolyticus DSM
RT 20540.";
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.
CC {ECO:0000256|ARBA:ARBA00004948}.
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DR EMBL; CP002537; ADY27203.1; -; Genomic_DNA.
DR RefSeq; WP_013622935.1; NC_015169.1.
DR AlphaFoldDB; F0RQ01; -.
DR KEGG; dpt:Deipr_2072; -.
DR HOGENOM; CLU_020520_0_0_0; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000007718; Plasmid pDEIPR01.
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 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADY27203.1};
KW Plasmid {ECO:0000313|EMBL:ADY27203.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007718};
KW Transferase {ECO:0000313|EMBL:ADY27203.1}.
FT DOMAIN 13..239
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 247 AA; 24806 MW; D42DDCA0FE7E098D CRC64;
MNKKIVLTIA GSDSGGGAGL QADLKTFQAF GVFGTSAVTL VTAQNTLGVQ QVFPLPPAVV
AAQIASVLSD LPPHAIKIGA LGQADIIQAV AAELREVRVP IILDPVMVAK GGSPLLSPDA
VAALTADLLP LATLVTPNLP EAAALGAGVL AGRDHLLKGG HGTGEVLEDV LHWQGHIFRF
PTPRQHTRHT HGTGCTLSSA IAAGLALGLE MPQAVAQAQA YVARALAAAP GLGGGHGPLE
HGVAVPG
//
