ID A0A014NJH6_9BURK Unreviewed; 288 AA.
AC A0A014NJH6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:EXU79593.1};
GN ORFNames=AX13_03815 {ECO:0000313|EMBL:EXU79593.1};
OS Comamonas aquatica DA1877.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=1457173 {ECO:0000313|EMBL:EXU79593.1, ECO:0000313|Proteomes:UP000020766};
RN [1] {ECO:0000313|EMBL:EXU79593.1, ECO:0000313|Proteomes:UP000020766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA1877 {ECO:0000313|EMBL:EXU79593.1,
RC ECO:0000313|Proteomes:UP000020766};
RA Watson E., Macneil L.T., Ritter A.D., Yilmaz L.S., Rosebrock A.P.,
RA Caudy A.A., Walhout A.J.;
RT "Interspecies Systems Biology Uncovers Metabolites Affecting C. elegans
RT Gene Expression and Life History Traits.";
RL Submitted (JAN-2014) 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}.
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:EXU79593.1}.
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DR EMBL; JBOK01000014; EXU79593.1; -; Genomic_DNA.
DR RefSeq; WP_043384610.1; NZ_JBOK01000014.1.
DR AlphaFoldDB; A0A014NJH6; -.
DR STRING; 225991.MA05_12290; -.
DR PATRIC; fig|1457173.3.peg.2429; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000020766; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; IPR001995; Peptidase_A2_cat.
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.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EXU79593.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020766};
KW Transferase {ECO:0000313|EMBL:EXU79593.1}.
FT DOMAIN 176..198
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
SQ SEQUENCE 288 AA; 29726 MW; 956DB3BF0DFB7C95 CRC64;
MTTQPLPHGS ASPRFPRYAR VLSIAGSDSG GGAGIQADLK TFSALGCYGM TAITAITAQN
TLGVRGIHGV PPEMLQAQID AVVQDIGVDA IKIGMLHAPE IVQVVADAIR RYGIANVVLD
PVMVATSGDK LIHDETVAVL VRELFPLASV ITPNLDEAGW LIGRKIADVA DMASAAQALL
DMGAQQVLLK GGHLPGDWVV DLLAGRDGAR QELGSQRIPT HNGHGTGCTL SSAIAAYLAR
GLPLPAAVES ARSYILGAIA AGAEVYTGRG HGPLNHGFAP QAQLVFTG
//
