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Database: UniProt
Entry: L7UJE9_MYXSD
LinkDB: L7UJE9_MYXSD
Original site: L7UJE9_MYXSD 
ID   L7UJE9_MYXSD            Unreviewed;       274 AA.
AC   L7UJE9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AGC46574.1};
GN   OrderedLocusNames=MYSTI_05294 {ECO:0000313|EMBL:AGC46574.1};
OS   Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Myxococcaceae; Myxococcus.
OX   NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC46574.1, ECO:0000313|Proteomes:UP000011131};
RN   [1] {ECO:0000313|EMBL:AGC46574.1, ECO:0000313|Proteomes:UP000011131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC   {ECO:0000313|Proteomes:UP000011131};
RX   PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA   Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT   "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT   fruiting myxobacterium.";
RL   Genome Announc. 1:E0010013-E0010013(2013).
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; CP004025; AGC46574.1; -; Genomic_DNA.
DR   AlphaFoldDB; L7UJE9; -.
DR   STRING; 1278073.MYSTI_05294; -.
DR   KEGG; msd:MYSTI_05294; -.
DR   PATRIC; fig|1278073.3.peg.5369; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_0_7; -.
DR   OMA; DNRHTHG; -.
DR   OrthoDB; 9810880at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000011131; 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:AGC46574.1};
KW   Transferase {ECO:0000313|EMBL:AGC46574.1}.
FT   DOMAIN          20..264
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   274 AA;  29013 MW;  C4A24873C3E5CDA8 CRC64;
     MRRMQTSSSV PTALTIAGSD SGGGAGIQAD LNTFSYHRVH GTTALTAITA QNTRGVTRVD
     VMPAEAVAAQ MDAVAEDLRV GAVKTGMLVN ADIISVVAWR LKSLKLGALV VDPVMVSRAG
     ARLIDDSAVG ALKQHLLPLA DIVTPNRHEA ELLAGLELRT LEDMQEAARR IHQLGPRAVL
     VKGGGMTGEL RGLDVWFDGE RMETLFLRAV KTQNTHGTGC TLSAAITAGL ALGQDAREAT
     RRAKEFVTAA LEHPLHLGQG HGPFSHFSPL NRPA
//
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