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Database: UniProt
Entry: L0ETW5_LIBCB
LinkDB: L0ETW5_LIBCB
Original site: L0ETW5_LIBCB 
ID   L0ETW5_LIBCB            Unreviewed;       266 AA.
AC   L0ETW5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AGA64078.1};
DE            EC=2.7.4.7 {ECO:0000313|EMBL:AGA64078.1};
GN   OrderedLocusNames=B488_00850 {ECO:0000313|EMBL:AGA64078.1};
OS   Liberibacter crescens (strain BT-1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA64078.1, ECO:0000313|Proteomes:UP000010799};
RN   [1] {ECO:0000313|EMBL:AGA64078.1, ECO:0000313|Proteomes:UP000010799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-1 {ECO:0000313|EMBL:AGA64078.1,
RC   ECO:0000313|Proteomes:UP000010799};
RX   PubMed=23408754; DOI=10.4056/sigs.3326772;
RA   Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J., Triplett E.W.;
RT   "Complete genome sequence of Liberibacter crescens BT-1.";
RL   Stand. Genomic Sci. 7:271-283(2012).
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; CP003789; AGA64078.1; -; Genomic_DNA.
DR   RefSeq; WP_015272505.1; NC_019907.1.
DR   AlphaFoldDB; L0ETW5; -.
DR   STRING; 1215343.B488_00850; -.
DR   KEGG; lcc:B488_00850; -.
DR   PATRIC; fig|1215343.11.peg.90; -.
DR   eggNOG; COG0351; Bacteria.
DR   HOGENOM; CLU_020520_0_1_5; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000010799; Chromosome.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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:AGA64078.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010799};
KW   Transferase {ECO:0000313|EMBL:AGA64078.1}.
FT   DOMAIN          12..250
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   266 AA;  28894 MW;  2239C6FC1C7290C5 CRC64;
     MTANAVTIAG SDSIGGAGIQ ADLKTFSALG VYGATVITAI TAQNIKTIRR IENVSSHMVS
     EQMEAVFTGL SIKAVKVGMV SSKKNIIAIA EGLSRFKNMA IIDPVMISSS GYILLDKKNI
     SVFKKELLPL ALMLTPNLEE AAFLTGEEKA LSEASMKRQA EKILKLGAQS VLLKGGHFHN
     PEESVDIFFN GKTFERLISP RIKKIQTHGT GCTLSAAITA YLAKGETILD AARKAKTYLY
     KSLESTKKLK ISHTGISLHH FHEWWD
//
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