ID D2Z7U9_9BACT Unreviewed; 271 AA.
AC D2Z7U9;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Phosphomethylpyrimidine kinase {ECO:0000313|EMBL:EFC91546.1};
GN ORFNames=Dpep_1520 {ECO:0000313|EMBL:EFC91546.1};
OS Dethiosulfovibrio peptidovorans DSM 11002.
OC Bacteria; Synergistota; Synergistia; Synergistales;
OC Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91546.1, ECO:0000313|Proteomes:UP000006427};
RN [1] {ECO:0000313|EMBL:EFC91546.1, ECO:0000313|Proteomes:UP000006427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91546.1,
RC ECO:0000313|Proteomes:UP000006427};
RX PubMed=21304695;
RA Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT strain (SEBR 4207).";
RL Stand. Genomic Sci. 3:85-92(2010).
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:EFC91546.1}.
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DR EMBL; ABTR02000001; EFC91546.1; -; Genomic_DNA.
DR AlphaFoldDB; D2Z7U9; -.
DR STRING; 469381.Dpep_1520; -.
DR PaxDb; 469381-Dpep_1520; -.
DR eggNOG; COG0351; Bacteria.
DR Proteomes; UP000006427; 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:EFC91546.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW Transferase {ECO:0000313|EMBL:EFC91546.1}.
FT DOMAIN 15..258
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 271 AA; 28117 MW; 5B289640186049E3 CRC64;
MSIYRGLAMT VAGSDSGGGA GIQADLKTFA ALRVFGTSAL TAVTAQNSLG VQAIHDIPPE
IIYEQMKSVL SDFSIGAVKT GMLGKTDAIG VVCRAVRDFS VHKLVVDPVM IAQSGDSLIQ
DDAVSAIKEE LLPLATLVTP NVPEAERLSG LEVSDVEGMI AAASAIAGMG PQAVLVKGGH
LEGEKVVDVL WSSGKPIKFE SPRIDTENNH GTGCTLSAAI ASELAAGCEL DLAVERGRAY
LMMALERGFK PGKGYGPTGH AVTPDWVKKG E
//
