ID E3CXM1_9BACT Unreviewed; 270 AA.
AC E3CXM1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Hydroxymethylpyrimidine kinasephosphomethylpyrimidine kinase {ECO:0000313|EMBL:EFQ24465.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:EFQ24465.1};
GN ORFNames=Apau_2054 {ECO:0000313|EMBL:EFQ24465.1};
OS Aminomonas paucivorans DSM 12260.
OC Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC Aminomonas.
OX NCBI_TaxID=584708 {ECO:0000313|EMBL:EFQ24465.1, ECO:0000313|Proteomes:UP000005096};
RN [1] {ECO:0000313|EMBL:EFQ24465.1, ECO:0000313|Proteomes:UP000005096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12260 {ECO:0000313|EMBL:EFQ24465.1,
RC ECO:0000313|Proteomes:UP000005096};
RX PubMed=21304733;
RA Pitluck S., Yasawong M., Held B., Lapidus A., Nolan M., Copeland A.,
RA Lucas S., Del Rio T.G., Tice H., Cheng J.F., Chertkov O., Goodwin L.,
RA Tapia R., Han C., Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Pukall R., Spring S., Rohde M., Sikorski J., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Non-contiguous finished genome sequence of Aminomonas paucivorans type
RT strain (GLU-3).";
RL Stand. Genomic Sci. 3:285-293(2010).
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; CM001022; EFQ24465.1; -; Genomic_DNA.
DR RefSeq; WP_006301705.1; NZ_CM001022.1.
DR AlphaFoldDB; E3CXM1; -.
DR STRING; 584708.Apau_2054; -.
DR PaxDb; 584708-Apau_2054; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_3_0; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000005096; 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 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:EFQ24465.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005096};
KW Transferase {ECO:0000313|EMBL:EFQ24465.1}.
FT DOMAIN 15..256
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 270 AA; 27942 MW; 9C80626002ECEBC9 CRC64;
MGLYRGVALT VAGSDSGGGA GIQADLKTFA ALRVFGTSAL AAVTVQNSLG VRGFHPVPEE
TVRGQIDAVC SDFPVGAVKT GMLASQALVR ATAEALEAAG VRNLVVDPVM VSQSGDPLLG
EDAAAALRDR LLPLALLATP NLPEAEVLLG RRIPGPEAME EAARDLLALG PKGVLLKGGH
LEGEELVDVL ALPGDLRVFR QSRLHTENTH GTGCTLSAAV AAELAAGCDL PEAVDRGRRY
LRQALEAGVR YGRGHGCPGH GVTPSWVDRR
//
