ID A0A374CDV7_9BACT Unreviewed; 312 AA.
AC A0A374CDV7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase {ECO:0000313|EMBL:RGH44664.1};
DE EC=2.7.1.49 {ECO:0000313|EMBL:RGH44664.1};
DE EC=2.7.4.7 {ECO:0000313|EMBL:RGH44664.1};
GN Name=thiD {ECO:0000313|EMBL:RGH44664.1};
GN ORFNames=DW917_04400 {ECO:0000313|EMBL:RGH44664.1};
OS Prevotella sp. AM42-24.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2293125 {ECO:0000313|EMBL:RGH44664.1, ECO:0000313|Proteomes:UP000263324};
RN [1] {ECO:0000313|EMBL:RGH44664.1, ECO:0000313|Proteomes:UP000263324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM42-24 {ECO:0000313|EMBL:RGH44664.1,
RC ECO:0000313|Proteomes:UP000263324};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RGH44664.1}.
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DR EMBL; QTXV01000008; RGH44664.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A374CDV7; -.
DR Proteomes; UP000263324; 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:RGH44664.1};
KW Transferase {ECO:0000313|EMBL:RGH44664.1}.
FT DOMAIN 14..289
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 312 AA; 33567 MW; EBFEE2FEC811A9A7 CRC64;
MKRYYTALTI AGSDSCGGAG IQADIKTMSA LGVYASSAIS AITVQNTTGV FGIQKVEPEI
VSGQIEAVMD DIHPQAIKIG MVNDGETIHA IAETLKKYLT AAPDKQQASA PTRSFQLIID
PVMVSTSGCR LMQEDALEIF IQELLPLASL LTPNIPEAEI LAGRKIQNVD DIRKAAASII
QLGCNNVLIK GGHFEGTEKM DYLFENKQHQ EANKQEHTGD IRETAIYKGA TVNTCNTHGT
GCTLSSAITS YLARGYNMEE AISSAKAYLS DAIEAGKDVK IGEGHGPVNH FHAPQKLYIL
TDEPIISDKT EK
//
