ID V4NDA3_9CAUL Unreviewed; 260 AA.
AC V4NDA3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ESQ79902.1};
GN ORFNames=AEYBE204_08630 {ECO:0000313|EMBL:ESQ79902.1};
OS Asticcacaulis sp. YBE204.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282363 {ECO:0000313|EMBL:ESQ79902.1, ECO:0000313|Proteomes:UP000017808};
RN [1] {ECO:0000313|EMBL:ESQ79902.1, ECO:0000313|Proteomes:UP000017808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBE204 {ECO:0000313|EMBL:ESQ79902.1,
RC ECO:0000313|Proteomes:UP000017808};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
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:ESQ79902.1}.
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DR EMBL; AWGF01000004; ESQ79902.1; -; Genomic_DNA.
DR RefSeq; WP_023462020.1; NZ_AWGF01000004.1.
DR AlphaFoldDB; V4NDA3; -.
DR STRING; 1282363.AEYBE204_08630; -.
DR PATRIC; fig|1282363.3.peg.1708; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000017808; 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 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:ESQ79902.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017808};
KW Transferase {ECO:0000313|EMBL:ESQ79902.1}.
FT DOMAIN 11..254
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 260 AA; 26804 MW; 9726EF8C04B61EB2 CRC64;
MRRVLIIAGS DPSGGAGIQA DLKAVTCLGG YGMTAITALT VQNTLGVTDV MPVPEAIITA
QGRACLSDIG ADAIKTGMLG TIPVVETVAA LIDEAPDAFI VVDPVMVAKG GHPLLPSEAI
SAIRSVLIPR AGLLTPNAPE AAVLTGIEVV DENSQRKAGE ALLKLGAKAV LMKGGHIDGD
EVVDWLMTPD GGERYSAKRV ETRHTHGTGC TLASACATLI TSERPLSESV GMARDYVLGA
ILMAPNLGHG HGPLRHNWVL
//