ID A0A426CDU9_9BACT Unreviewed; 275 AA.
AC A0A426CDU9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:RRJ94271.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:RRJ94271.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:RRJ94271.1};
GN Name=thiD {ECO:0000313|EMBL:RRJ94271.1};
GN ORFNames=Ga0100231_007765 {ECO:0000313|EMBL:RRJ94271.1};
OS Opitutaceae bacterium TAV4.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae.
OX NCBI_TaxID=278959 {ECO:0000313|EMBL:RRJ94271.1, ECO:0000313|Proteomes:UP000078325};
RN [1] {ECO:0000313|EMBL:RRJ94271.1, ECO:0000313|Proteomes:UP000078325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAV4 {ECO:0000313|EMBL:RRJ94271.1,
RC ECO:0000313|Proteomes:UP000078325};
RA Rodrigues J., Kotak M., Lin J.;
RT "Draft genome sequences of strains TAV3 and TAV4 (Verrucomicrobial:
RT Opitutaceae) isolated from a wood-feeding termite and in silico analysis of
RT their polysaccharide-degrading enzymes.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRJ94271.1}.
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DR EMBL; LXWU02000003; RRJ94271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A426CDU9; -.
DR STRING; 278959.Ga0100231_00800; -.
DR Proteomes; UP000078325; Unassembled WGS sequence.
DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC.
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:RRJ94271.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078325};
KW Transferase {ECO:0000313|EMBL:RRJ94271.1}.
FT DOMAIN 12..259
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 275 AA; 28993 MW; 09175DF32987F1B0 CRC64;
MIPNVLTIAG VDPSGGAGVL ADIKTFSALG AYGAGVIAAL TAQNTQGVTG VQAVPVEFIA
QQLDTLFADL RIDAVKLGML GDAATIATVA DGLRRHDVRR LVVDPVMVAK SGHHLLAREA
IAALREKILP LAEVLTPNLP EAAVLLNTPP PATLNEMRDA ARALHHLGPR IVMLKGGHLD
GPESIDIVDD GTTQHELRAP RTATRNTHGT GCTLSAAIAA LLPRHADPID AIRAAKHYIT
RAIAAADQLD VGHGHGPVHH FHSLWQQPRK PDMDK
//
