ID A1US06_BARBK Unreviewed; 252 AA.
AC A1US06;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ABM44655.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:ABM44655.1};
GN Name=thiD {ECO:0000313|EMBL:ABM44655.1};
GN OrderedLocusNames=BARBAKC583_0441 {ECO:0000313|EMBL:ABM44655.1};
OS Bartonella bacilliformis (strain ATCC 35685 / KC583 / Herrer 020/F12,63).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=360095 {ECO:0000313|EMBL:ABM44655.1, ECO:0000313|Proteomes:UP000000643};
RN [1] {ECO:0000313|EMBL:ABM44655.1, ECO:0000313|Proteomes:UP000000643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35685 / NCTC 12138 / KC583
RC {ECO:0000313|Proteomes:UP000000643};
RA Hendrix L., Mohamoud Y., Radune D., Shvartsbeyn A., Daugherty S.,
RA Dodson R., Durkin A.S., Harkins D., Huot H., Kothari S.P., Madupu R.,
RA Li J., Nelson W.C., Shrivastava S., Giglio M.G., Haft D., Selengut J.,
RA Fraser-Ligget C., Seshadri R.;
RL Submitted (DEC-2006) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000524; ABM44655.1; -; Genomic_DNA.
DR RefSeq; WP_005766483.1; NC_008783.1.
DR AlphaFoldDB; A1US06; -.
DR STRING; 360095.BARBAKC583_0441; -.
DR GeneID; 72471954; -.
DR KEGG; bbk:BARBAKC583_0441; -.
DR PATRIC; fig|360095.6.peg.423; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_2_5; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000000643; 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:ABM44655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000643};
KW Transferase {ECO:0000313|EMBL:ABM44655.1}.
FT DOMAIN 14..246
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 252 AA; 26881 MW; 2BD411AF4678D5F6 CRC64;
MALIPSILVV AGTDPTGGAG IVRDIETTAH FQIKASLAIT SVNVQNNNHV AEIAPMSGKF
VAAQMQVALE ANPISAIKIG MTGTQEIIAE ICNILKNYNH IPVVLDPVFV ASSGGRLTTE
KIIEIMNNKL LPHIDILTPN MKELALLSQS PLASNHQEAM QQAKKLLSLG PRYILVKGGH
ADGPFATDSL ISQTEVINIS APRLKGTMRG TGCILSSAIA TRLALNETMT DAVKNAKAYI
HTLLLTHCQK DH
//
