ID A0A0R2GXJ8_9LACO Unreviewed; 266 AA.
AC A0A0R2GXJ8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00019161};
DE EC=2.7.1.49 {ECO:0000256|ARBA:ARBA00012135};
DE EC=2.7.4.7 {ECO:0000256|ARBA:ARBA00012963};
DE AltName: Full=Hydroxymethylpyrimidine kinase {ECO:0000256|ARBA:ARBA00042102};
DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase {ECO:0000256|ARBA:ARBA00043176};
GN ORFNames=IV41_GL000721 {ECO:0000313|EMBL:KRN45505.1};
OS Limosilactobacillus ingluviei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN45505.1, ECO:0000313|Proteomes:UP000051639};
RN [1] {ECO:0000313|EMBL:KRN45505.1, ECO:0000313|Proteomes:UP000051639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN45505.1,
RC ECO:0000313|Proteomes:UP000051639};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 2/3. {ECO:0000256|ARBA:ARBA00037917}.
CC -!- SIMILARITY: Belongs to the ThiD family.
CC {ECO:0000256|ARBA:ARBA00009879}.
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:KRN45505.1}.
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DR EMBL; JQBA01000002; KRN45505.1; -; Genomic_DNA.
DR RefSeq; WP_056993663.1; NZ_JQBA01000002.1.
DR AlphaFoldDB; A0A0R2GXJ8; -.
DR STRING; 1203076.GCA_000312405_00539; -.
DR PATRIC; fig|148604.4.peg.728; -.
DR eggNOG; COG0351; Bacteria.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000051639; 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 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 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:KRN45505.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051639};
KW Transferase {ECO:0000313|EMBL:KRN45505.1}.
FT DOMAIN 16..262
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 266 AA; 27879 MW; 404506F8CCCEA47B CRC64;
MTKPQFPQVL SIAGSDSGGG AGMQADLKTM QMRHVFATTV LVAITAQNAR GVQRAQVLPP
AMIDAQFAAL AEDLQIKAVK TGMLADSQTV QTVVQNLQRY DFGPLTVDPV MIAKGGAPLL
ADEAVATVRD QLLPLATLIT PNLPEAEVLT GQKIRTEAQM RQAAEHLQAL GAANVLVKGG
HLGADQAAVD YVLLANGRDF WLTSPRVATA NTHGTGDTIS ACITAELAKG VDLATAIRVA
KAYVTATIRE GIQVGHGHGP LNHWAV
//
