ID B9CYF9_CAMRE Unreviewed; 264 AA.
AC B9CYF9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:EEF15256.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:EEF15256.1};
GN Name=thiD {ECO:0000313|EMBL:EEF15256.1};
GN ORFNames=CAMRE0001_1779 {ECO:0000313|EMBL:EEF15256.1};
OS Campylobacter rectus RM3267.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF15256.1, ECO:0000313|Proteomes:UP000003082};
RN [1] {ECO:0000313|EMBL:EEF15256.1, ECO:0000313|Proteomes:UP000003082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM3267 {ECO:0000313|EMBL:EEF15256.1,
RC ECO:0000313|Proteomes:UP000003082};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (AUG-2008) 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 -!- 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:EEF15256.1}.
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DR EMBL; ACFU01000002; EEF15256.1; -; Genomic_DNA.
DR RefSeq; WP_002943993.1; NZ_ACFU01000002.1.
DR AlphaFoldDB; B9CYF9; -.
DR STRING; 553218.CAMRE0001_1779; -.
DR eggNOG; COG0351; Bacteria.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000003082; Unassembled WGS sequence.
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 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:EEF15256.1};
KW Transferase {ECO:0000313|EMBL:EEF15256.1}.
FT DOMAIN 11..255
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 264 AA; 28229 MW; 79F31BABA00EDFA2 CRC64;
MKHVLSIAGV DPSGGAGVIA DLKVFAAHGV YAMGAITALT AQNTKGIFDM QLVECDLIAK
QIEAIFDDIR VDAVKIGVVP SEQIIKTVAA TLRKVSNLPP VVLDPVMSCK NGDIWLEGAA
KDAIVSELFP LSTVITPNKF EAREIVKREP KSKDEFKQAC KELLKTGAKS VYLKCGDVGG
VSLDLFYDGA EFTEFEQERI DTSSTHGSGC SLSSAIASNL ALGFSLRESA QRANKYVYKA
IKAAFAVGSG CNPINHFHNV EFGD
//