ID R3WN35_9ENTE Unreviewed; 276 AA.
AC R3WN35;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=pyridoxal kinase {ECO:0000256|ARBA:ARBA00012104};
DE EC=2.7.1.35 {ECO:0000256|ARBA:ARBA00012104};
DE AltName: Full=PN/PL/PM kinase {ECO:0000256|ARBA:ARBA00042348};
DE AltName: Full=Pyridoxal kinase {ECO:0000256|ARBA:ARBA00042396};
DE AltName: Full=Pyridoxamine kinase {ECO:0000256|ARBA:ARBA00042307};
DE AltName: Full=Vitamin B6 kinase {ECO:0000256|ARBA:ARBA00042531};
GN ORFNames=UC7_02594 {ECO:0000313|EMBL:EOL43265.1};
OS Enterococcus caccae ATCC BAA-1240.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158612 {ECO:0000313|EMBL:EOL43265.1, ECO:0000313|Proteomes:UP000013840};
RN [1] {ECO:0000313|EMBL:EOL43265.1, ECO:0000313|Proteomes:UP000013840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1240 {ECO:0000313|EMBL:EOL43265.1,
RC ECO:0000313|Proteomes:UP000013840};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus caccae BAA-1240.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate;
CC Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326;
CC EC=2.7.1.35; Evidence={ECO:0000256|ARBA:ARBA00036247};
CC -!- SIMILARITY: Belongs to the ThiD family.
CC {ECO:0000256|ARBA:ARBA00009879}.
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:EOL43265.1}.
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DR EMBL; AJAU01000022; EOL43265.1; -; Genomic_DNA.
DR RefSeq; WP_010772680.1; NZ_KE136472.1.
DR AlphaFoldDB; R3WN35; -.
DR STRING; 317735.RU98_GL003209; -.
DR PATRIC; fig|1158612.3.peg.2557; -.
DR eggNOG; COG0351; Bacteria.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000013840; 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; PHOSPHOMETHYLPYRIMIDINE KINASE; 1.
DR PANTHER; PTHR20858:SF19; PYRIDOXINE KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EOL43265.1};
KW Transferase {ECO:0000313|EMBL:EOL43265.1}.
FT DOMAIN 12..257
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 276 AA; 29579 MW; 6B5579D27EA20EC3 CRC64;
MIKKVLTVAG SDSSGGAGIQ ADLKTFEEYG TFGFSALTSI VTMDPDEGWS HLVTPIEPEL
VEKQLKTIFA GGALDAMKTG MLGTIESIEI TRTYIDKFSM NNIVIDPVMA CKGTSELLQP
ENVAAMTRLL LPKATITTPN LVEAGILSGM GELTSVDQMK EAAKKIIDLG PKNVVIKGGH
RLKTDQAIDL FYDGTDFTIF ESQLFPTDYN HGAGCTFAAS VTAGLAKGYS VADAVALAKK
FVAAAIENGQ KINPFLGHVW HGAYNHAENR MTEIKE
//
