ID B5YFN2_THEYD Unreviewed; 254 AA.
AC B5YFN2;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:ACI21605.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:ACI21605.1};
GN Name=thiD {ECO:0000313|EMBL:ACI21605.1};
GN OrderedLocusNames=THEYE_A1264 {ECO:0000313|EMBL:ACI21605.1};
OS Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87).
OC Bacteria; Nitrospirota; Thermodesulfovibrionia; Thermodesulfovibrionales;
OC Thermodesulfovibrionaceae; Thermodesulfovibrio.
OX NCBI_TaxID=289376 {ECO:0000313|EMBL:ACI21605.1, ECO:0000313|Proteomes:UP000000718};
RN [1] {ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RA Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT "The complete genome sequence of Thermodesulfovibrio yellowstonii strain
RT ATCC 51303 / DSM 11347 / YP87.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI21605.1, ECO:0000313|Proteomes:UP000000718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51303 / DSM 11347 / YP87
RC {ECO:0000313|Proteomes:UP000000718};
RX PubMed=25635016;
RA Bhatnagar S., Badger J.H., Madupu R., Khouri H.M., O'Connor E.M.,
RA Robb F.T., Ward N.L., Eisen J.A.;
RT "Genome Sequence of the Sulfate-Reducing Thermophilic Bacterium
RT Thermodesulfovibrio yellowstonii Strain DSM 11347T (Phylum Nitrospirae).";
RL Genome Announc. 3:0-0(2015).
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; CP001147; ACI21605.1; -; Genomic_DNA.
DR RefSeq; WP_012546315.1; NC_011296.1.
DR RefSeq; YP_002249080.1; NC_011296.1.
DR AlphaFoldDB; B5YFN2; -.
DR STRING; 289376.THEYE_A1264; -.
DR EnsemblBacteria; ACI21605; ACI21605; THEYE_A1264.
DR KEGG; tye:THEYE_A1264; -.
DR PATRIC; fig|289376.4.peg.1235; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_0; -.
DR InParanoid; B5YFN2; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000000718; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009228; P:thiamine biosynthetic process; IBA:GO_Central.
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:ACI21605.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000718};
KW Transferase {ECO:0000313|EMBL:ACI21605.1}.
FT DOMAIN 11..250
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 254 AA; 27915 MW; C5CF42823A42A0BE CRC64;
MKIALTIGAS DPTSGAGIQM DLKVFHSLEV YGLSILTAVT AQSTIEFSSV FPLPEEIINS
QFETLLKDLK PHGTKIGMIY SKEAFQCVIS NIKNLNIKNL VIDPVMTSTL GAKLLENNAL
KTLKEELIPL SMAVTANIPE AEALTELKIE RIEDLYEASK QLYQMGTKFA IIKGGHFEKK
AIDILYDGKN FYKIDGKKIP GQFHGTGCAF SSAFVCFLCK GYNPLEAFKA SKDFVRKAIE
NSLKLGQGIN LLII
//
