ID E6YGU4_BARC7 Unreviewed; 249 AA.
AC E6YGU4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:CBI76082.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:CBI76082.1};
GN Name=thiD {ECO:0000313|EMBL:CBI76082.1};
GN OrderedLocusNames=BARCL_0401 {ECO:0000313|EMBL:CBI76082.1};
OS Bartonella clarridgeiae (strain CCUG 45776 / CIP 104772 / 73).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=696125 {ECO:0000313|EMBL:CBI76082.1, ECO:0000313|Proteomes:UP000009101};
RN [1] {ECO:0000313|Proteomes:UP000009101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RA Engel P., Salzburger W., Marius L., Chao-Chin C., Soichi M., Christa L.,
RA Alexandra C., Aurelie L., Claudine M., Stephan S.C., Christoph D.;
RT "Genome sequencing of Bartonella species and comparative genomics.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBI76082.1, ECO:0000313|Proteomes:UP000009101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 104772 / 73 {ECO:0000313|Proteomes:UP000009101};
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(2011).
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; FN645454; CBI76082.1; -; Genomic_DNA.
DR AlphaFoldDB; E6YGU4; -.
DR STRING; 696125.BARCL_0401; -.
DR KEGG; bcd:BARCL_0401; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_2_5; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000009101; Chromosome.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:RHEA.
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 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:CBI76082.1};
KW Transferase {ECO:0000313|EMBL:CBI76082.1}.
FT DOMAIN 11..244
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 249 AA; 26832 MW; 397C6953AF9F3C16 CRC64;
MSSILIVAGT DPTGGAGIVR DIETATYFQT KASLAITAVN VQDNNHVAEI IPMSRETIAA
QMRVALKNNS IHAIKIGMTG TQAIIEGICD ILKDYHHIPT VLDPVLIASS GGQLTTEKII
DIMLNKLFPH IDLLTPNMVE LALLSQSPLA SNHEEAIQQA QKLLSFGPRH ILIKGGHIEG
NFATDSLIDK TEVINISSPR LKGTMRGTGC ILSSAIAAHL ALKQSMIEAI KNAKAYTYTL
LLKHCQKNL
//
