ID A0A0S8CF88_9CHLR Unreviewed; 265 AA.
AC A0A0S8CF88;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:KPK22132.1};
GN ORFNames=AMJ76_00665 {ECO:0000313|EMBL:KPK22132.1};
OS Dehalococcoidia bacterium SM23_28_1.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703395 {ECO:0000313|EMBL:KPK22132.1, ECO:0000313|Proteomes:UP000054497};
RN [1] {ECO:0000313|EMBL:KPK22132.1, ECO:0000313|Proteomes:UP000054497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_28_1 {ECO:0000313|EMBL:KPK22132.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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}.
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:KPK22132.1}.
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DR EMBL; LJTZ01000008; KPK22132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CF88; -.
DR PATRIC; fig|1703395.3.peg.74; -.
DR Proteomes; UP000054497; Unassembled WGS sequence.
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; 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:KPK22132.1};
KW Transferase {ECO:0000313|EMBL:KPK22132.1}.
FT DOMAIN 12..256
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 265 AA; 27710 MW; 60C99A44E20DF1A1 CRC64;
MKTTVMTIAG SDSSGGAGIQ ADLKTFAALG VYGACAITAV TAQDSTRVWA IHELPPELVA
AQIDAVVQDM GVDAVKTGML ASAGIVRVVA ERVRQHRLPN VVVDPVLAAK SGDRLLREDA
VSVLRAELLP LCTVVTPNIP EAEVLAGYRL ETDEDLQRAA QEIAALGARN VVITGGHASG
PEAVDLLYDG RGFRRFSAPR LATRHGRGAG CTFASAIAAL LAQGAGIEEA VARAKEYTAA
ALEHAFALGK GPGPVHHFYR WWEGG
//
