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Database: UniProt
Entry: A0A0Q5CN54_9BURK
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Original site: A0A0Q5CN54_9BURK 
ID   A0A0Q5CN54_9BURK        Unreviewed;       266 AA.
AC   A0A0Q5CN54;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:KQQ33746.1};
GN   ORFNames=ASF61_11930 {ECO:0000313|EMBL:KQQ33746.1};
OS   Duganella sp. Leaf126.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ33746.1, ECO:0000313|Proteomes:UP000051032};
RN   [1] {ECO:0000313|EMBL:KQQ33746.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33746.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ33746.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33746.1};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQQ33746.1}.
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DR   EMBL; LMNW01000031; KQQ33746.1; -; Genomic_DNA.
DR   RefSeq; WP_056157834.1; NZ_LMNW01000031.1.
DR   AlphaFoldDB; A0A0Q5CN54; -.
DR   STRING; 1736266.ASF61_11930; -.
DR   OrthoDB; 9810880at2; -.
DR   UniPathway; UPA00060; UER00138.
DR   Proteomes; UP000051032; Unassembled WGS sequence.
DR   GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
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:KQQ33746.1};
KW   Transferase {ECO:0000313|EMBL:KQQ33746.1}.
FT   DOMAIN          25..260
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   266 AA;  27160 MW;  726D3CFDF2296463 CRC64;
     MVSITARMAA TPLQHPCVLV FAGLDPSGGA GLVADAQAVV AQGAHALTVC TALTVQDNDR
     VFAVEPVAAE LVLRQARALT AKITIGAVKI GIPGSAANAL AIAEVIQELR ATHAQLPVVL
     DPVLASGHGD VLTPGDAVAA LAPLLPLVTV LTPNGPEAHR LTGVHDVAAQ AAVLGGQGCR
     NVLVTGGHGA GPTLVNHCYG DVRHRWQWPR LPGQFHGSGC TLAAAIAGRL ALGLPVLAAL
     EQAQHYCFTA LRDAYAVAPG QRMPLR
//
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