ID A0A0R2EQU0_9LACO Unreviewed; 277 AA.
AC A0A0R2EQU0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=FC75_GL000606 {ECO:0000313|EMBL:KRN18665.1};
OS Lacticaseibacillus camelliae DSM 22697 = JCM 13995.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423730 {ECO:0000313|EMBL:KRN18665.1, ECO:0000313|Proteomes:UP000050865};
RN [1] {ECO:0000313|EMBL:KRN18665.1, ECO:0000313|Proteomes:UP000050865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22697 {ECO:0000313|EMBL:KRN18665.1,
RC ECO:0000313|Proteomes:UP000050865};
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:KRN18665.1}.
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DR EMBL; AYZJ01000085; KRN18665.1; -; Genomic_DNA.
DR RefSeq; WP_054666518.1; NZ_BBAJ01000137.1.
DR AlphaFoldDB; A0A0R2EQU0; -.
DR STRING; 1423730.FC75_GL000606; -.
DR PATRIC; fig|1423730.4.peg.629; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000050865; 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:KRN18665.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050865};
KW Transferase {ECO:0000313|EMBL:KRN18665.1}.
FT DOMAIN 15..262
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 277 AA; 29827 MW; C281A95D56EB122B CRC64;
MANELPQVAT IAGVDSDGSA GAQADLHSFF MRGTYGTLIL TAAVAGNSYG IHDSQVMPLS
FIDSQFKAVG EDLKIRAAKT GMLADSAVIK DVAANLKQYD FGPLVLDPVI STKHGNMLLE
TEAFETLKTV LIPMADVITP NFYEAEHLTG MKLTDKDAII KAAEAIHDMG AKNVMLKGRH
DSASQTEVSD YVLLDSGKSF WLTGPYYDTE RKNGTGDTLS AVITAELGKG TDLEDAIRLA
KHFVDTAIAH EIPVGHKFGP INHWANPLVQ PSQRPED
//
