ID A0A098LMN7_9BACT Unreviewed; 251 AA.
AC A0A098LMN7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:GAL87353.1};
GN ORFNames=MYP_4583 {ECO:0000313|EMBL:GAL87353.1};
OS Sporocytophaga myxococcoides.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Sporocytophaga.
OX NCBI_TaxID=153721 {ECO:0000313|EMBL:GAL87353.1, ECO:0000313|Proteomes:UP000030185};
RN [1] {ECO:0000313|EMBL:GAL87353.1, ECO:0000313|Proteomes:UP000030185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-01 {ECO:0000313|EMBL:GAL87353.1,
RC ECO:0000313|Proteomes:UP000030185};
RA Liu L., Gao P.J., Chen G.J., Wang L.S.;
RT "Sporocytophaga myxococcoides PG-01 genome sequencing.";
RL Submitted (SEP-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:GAL87353.1}.
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DR EMBL; BBLT01000012; GAL87353.1; -; Genomic_DNA.
DR RefSeq; WP_045468614.1; NZ_BBLT01000012.1.
DR AlphaFoldDB; A0A098LMN7; -.
DR STRING; 153721.MYP_4583; -.
DR eggNOG; COG0351; Bacteria.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000030185; Unassembled WGS sequence.
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 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 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:GAL87353.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030185};
KW Transferase {ECO:0000313|EMBL:GAL87353.1}.
FT DOMAIN 15..245
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 251 AA; 28057 MW; D7B80FC567B40AAE CRC64;
MNRIRTKVLS IAGFDPSAGA GVLADIKTFE SHKVYGFGVV SSLTVQNEKE FLSNQWIPVD
AILQQIDVLL KEHKVEFVKI GLVESYDVLL KLTEALKGYN PKIKIIWDPV IKASAGFTFH
EDQNQEKISK ACSALHMITP NWQEIQFLVP EKDPMEAGKY LSRFCNVYLK GGHNSKDEAR
DYLFSMDGKV FPFKPKTIVE YPKHGSGCVL SSALTANLSK GYPLIKACIR AKDYITKFLA
SNQTLLGNHK G
//
