ID L0GT14_9GAMM Unreviewed; 267 AA.
AC L0GT14;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AGA88947.1};
GN ORFNames=Thimo_0071 {ECO:0000313|EMBL:AGA88947.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA88947.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA88947.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA88947.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) 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}.
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DR EMBL; CP003051; AGA88947.1; -; Genomic_DNA.
DR RefSeq; WP_015279097.1; NC_019940.1.
DR AlphaFoldDB; L0GT14; -.
DR STRING; 765912.Thimo_0071; -.
DR KEGG; tmb:Thimo_0071; -.
DR PATRIC; fig|765912.4.peg.68; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_2_6; -.
DR OrthoDB; 9810880at2; -.
DR UniPathway; UPA00060; UER00138.
DR Proteomes; UP000010816; 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 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:AGA88947.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW Transferase {ECO:0000313|EMBL:AGA88947.1}.
FT DOMAIN 16..249
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 267 AA; 27976 MW; 8A6F3A09E2474C61 CRC64;
MSHPPVPIVL CAGGHDPTGG AGLTADTEAV RAVGAHALGL VTCLTTQDTC GLSGVFPQPA
EQIASQWRAL FNDSAVAAIK IGLLGSVAIA QGIEDLVRAH SDLPVVLDPV LASGAGDPLA
DAALIERLRH DVPGVCTLMT PNLPEAQTLT GEEDPEDCAA ALRRAGCRWV LITGTHAAEA
EVVNRLYGPD GRRQVWRWPR LPHHYHGSGC TLASAIAARL ASGDDLVEAV AAAQTYTWET
LARARRTGRC QLTPNRLFAL DAAADRA
//
