ID A6SXA9_JANMA Unreviewed; 273 AA.
AC A6SXA9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ABR88516.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:ABR88516.1};
GN Name=thiD1 {ECO:0000313|EMBL:ABR88516.1};
GN OrderedLocusNames=mma_1216 {ECO:0000313|EMBL:ABR88516.1};
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88516.1, ECO:0000313|Proteomes:UP000006388};
RN [1] {ECO:0000313|EMBL:ABR88516.1, ECO:0000313|Proteomes:UP000006388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille {ECO:0000313|EMBL:ABR88516.1,
RC ECO:0000313|Proteomes:UP000006388};
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88516.1; -; Genomic_DNA.
DR AlphaFoldDB; A6SXA9; -.
DR STRING; 375286.mma_1216; -.
DR KEGG; mms:mma_1216; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_2_4; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000006388; 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:ABR88516.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006388};
KW Transferase {ECO:0000313|EMBL:ABR88516.1}.
FT DOMAIN 25..261
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 273 AA; 28783 MW; 7C6329E54B4EF921 CRC64;
MFKESISTMN TSSSRPVVLC LSGHDPSGGA GLQADIEALM AQGCHAAPTV TALTVQNSVD
VSDFRVLDSA WVLAQAEAVI TDLPIAGIKL GMLGSVEMVD TVAGILQRLP NVPVVCDPVL
RAGGGGALGK DEVGYAMRER LLPLATIVTP NLPEARILAE LPNGTADECA AKLLPFCQHL
LITGGHGDEQ QVHNRLYSRD GSSHTFTCDR LPGSYHGSGC TLASTLAGRL ALGEATVEAV
ENALAYTWRT LRDADRSGKG QHFPRRLPLD FCA
//
