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Database: UniProt
Entry: A8AVB5_STRGC
LinkDB: A8AVB5_STRGC
Original site: A8AVB5_STRGC 
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
//
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