ID A0A087BPU0_9BIFI Unreviewed; 295 AA.
AC A0A087BPU0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:KFI73040.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:KFI73040.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:KFI73040.1};
GN ORFNames=BMIN_0758 {ECO:0000313|EMBL:KFI73040.1};
OS Bifidobacterium minimum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI73040.1, ECO:0000313|Proteomes:UP000029014};
RN [1] {ECO:0000313|EMBL:KFI73040.1, ECO:0000313|Proteomes:UP000029014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI73040.1,
RC ECO:0000313|Proteomes:UP000029014};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine
CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
CC {ECO:0000256|ARBA:ARBA00003848}.
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; 4-
CC amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-
CC ribosyl)imidazole: step 3/3. {ECO:0000256|ARBA:ARBA00004769}.
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:KFI73040.1}.
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DR EMBL; JGZD01000008; KFI73040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BPU0; -.
DR STRING; 1693.BMIN_0758; -.
DR eggNOG; COG0351; Bacteria.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000029014; Unassembled WGS sequence.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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:UniProtKB-KW.
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:KFI73040.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029014};
KW Transferase {ECO:0000313|EMBL:KFI73040.1}.
FT DOMAIN 15..261
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 295 AA; 30210 MW; 5882AA3A99987646 CRC64;
MTSPLASVLS IAGSDSLGGA GIQADLKTLI ACGVYGMSAI TSLTAQNTTG VFSTQNTSIS
MLDAQIRAVF DDIRPDAVKV GMIPTAPLVD VVARRLDSYA ATNVVVDTVM ISSSGTALID
RNAIDAVDAK LLPLATLITP NIAEAQTLLG LKPGSLGDPA AMEDAALALS SRYGTAILLK
GGHSAGNAND VLADRGRTTW FTSPRIDNPN THGTGCTLSS AIAAGLATGL TLPEAVASAK
AYTTGAIAAG LDLGQGNGPM DHAWRWHNEE ERRIAITRPQ AAGVSHQRAA AHDNT
//
