ID U5N9D2_9BURK Unreviewed; 277 AA.
AC U5N9D2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AGX88176.1};
GN Name=thiD {ECO:0000313|EMBL:AGX88176.1};
GN ORFNames=Cenrod_2105 {ECO:0000313|EMBL:AGX88176.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX88176.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX88176.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX88176.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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; CP004885; AGX88176.1; -; Genomic_DNA.
DR RefSeq; WP_022775258.1; NC_022576.1.
DR AlphaFoldDB; U5N9D2; -.
DR STRING; 946483.Cenrod_2105; -.
DR KEGG; cbx:Cenrod_2105; -.
DR PATRIC; fig|946483.4.peg.2121; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_3_4; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000017184; Chromosome.
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:AGX88176.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184};
KW Transferase {ECO:0000313|EMBL:AGX88176.1}.
FT DOMAIN 13..260
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
FT REGION 255..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 28705 MW; 0526780802B5051A CRC64;
MQYPRVLTIA GSDSGGGAGI QADLKTFAAL GCYGMSAITA LTAQNTCEVR SIHSVPPEML
REQIDAVVQD IGVCAVKVGM LHCAEIVHTV AHAIDRYVLP HVVLDPVMVA TSGAVLIDQR
AVETLVQQLF PRSAIVTPNL DEAALLVGKP LTSPQDMAEA AQALLGRGAH AVLLKGGHLP
GPTVTDLLLV HGQEPIWMAT PRIDTPNTHG TGCTLSSAIA AHLALGASLV DAVQRAHDFV
AQALRSGAAV RTGHGNGPLN HGFGPAPMRI LPDDAPA
//
