ID A8AVB5_STRGC Unreviewed; 253 AA.
AC A8AVB5;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
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 OrderedLocusNames=SGO_0409 {ECO:0000313|EMBL:ABV09285.1};
OS Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS DL1 / V288).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV09285.1, ECO:0000313|Proteomes:UP000001131};
RN [1] {ECO:0000313|EMBL:ABV09285.1, ECO:0000313|Proteomes:UP000001131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC {ECO:0000313|Proteomes:UP000001131};
RX PubMed=17720781; DOI=10.1128/JB.01023-07;
RA Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT to competence signaling peptide.";
RL J. Bacteriol. 189:7799-7807(2007).
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}.
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DR EMBL; CP000725; ABV09285.1; -; Genomic_DNA.
DR RefSeq; WP_011999921.1; NC_009785.1.
DR AlphaFoldDB; A8AVB5; -.
DR STRING; 467705.SGO_0409; -.
DR KEGG; sgo:SGO_0409; -.
DR eggNOG; COG0351; Bacteria.
DR HOGENOM; CLU_020520_0_0_9; -.
DR OMA; KDEVGYA; -.
DR Proteomes; UP000001131; Chromosome.
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 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:ABV09285.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001131};
KW Transferase {ECO:0000313|EMBL:ABV09285.1}.
FT DOMAIN 13..247
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 253 AA; 27445 MW; 03AD9E13C41B84D7 CRC64;
MKDKLILALS GNDIFSGGGL HADLATYTVN GLHGFVAVTC LTAMTNKGFE VIPVEEEVFA
QQLASLKDVP FSAIKIGLLP NLQIAEQALA FVKQHADIPV VLDPVLVCKE NHDLEVSALR
EEIIKFFPYV SIITPNLAEA QLLTQKEIKT LGDMQVAAKE LYDLGAKHVV IKGGNRLSKE
RAVDVYYDGR DFEVLESPVL ASNNTGAGCT FASSIASQLL LGKSPLAAVQ FSKDFVYGAI
QRSDQYGVVQ YEK
//