ID A0A109QJV8_9DEIN Unreviewed; 258 AA.
AC A0A109QJV8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:AMA75834.1};
GN ORFNames=AV541_07255 {ECO:0000313|EMBL:AMA75834.1};
OS Thermus parvatiensis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=456163 {ECO:0000313|EMBL:AMA75834.1, ECO:0000313|Proteomes:UP000061630};
RN [1] {ECO:0000313|EMBL:AMA75834.1, ECO:0000313|Proteomes:UP000061630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RL {ECO:0000313|EMBL:AMA75834.1,
RC ECO:0000313|Proteomes:UP000061630};
RA Tripathi C., Lal R.;
RT "Genome sequence of Thermus parvatiensis, a thermophile isolated from a hot
RT water spring.";
RL Submitted (JAN-2016) 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; CP014141; AMA75834.1; -; Genomic_DNA.
DR RefSeq; WP_060384599.1; NZ_CP014141.1.
DR AlphaFoldDB; A0A109QJV8; -.
DR KEGG; tpar:AV541_07255; -.
DR Proteomes; UP000061630; 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 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; IPR001763; Rhodanese-like_dom.
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.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AMA75834.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000061630};
KW Transferase {ECO:0000313|EMBL:AMA75834.1}.
FT DOMAIN 155..188
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 258 AA; 26642 MW; CB1134D8491735D6 CRC64;
MRVALTIAGS DSGGGAGVQA DLKVFFRFGV YGTSALTLVT AQNTLGVQRV HLLPPEVVYA
QIESVAQDFP LHAAKTGALG DGAIVEAVAD AVGRYGIAPL VVDPVMVAKS GDPLLAPEAV
AALKERLFPL AALITPNRLE AEALLGRPIR TLEEAEEAAK ALLALGPKAV LLKGGHLEGE
RAVDLLATQE GILRFSAPRV QTRNTHGTGC TLSAAIAALL AKGRPLAEAV AEAKAYLTRA
LKTAPSLGHG HGPLDHWA
//
