ID A0A239UG36_9STAP Unreviewed; 276 AA.
AC A0A239UG36;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=SPI02_22420 {ECO:0000313|EMBL:GEP85657.1};
OS Staphylococcus piscifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=70258 {ECO:0000313|EMBL:GEP85657.1, ECO:0000313|Proteomes:UP000321736};
RN [1] {ECO:0000313|EMBL:GEP85657.1, ECO:0000313|Proteomes:UP000321736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 109625 {ECO:0000313|EMBL:GEP85657.1,
RC ECO:0000313|Proteomes:UP000321736};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Staphylococcus piscifermentans NBRC
RT 109625.";
RL Submitted (JUL-2019) 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:GEP85657.1}.
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DR EMBL; BKAR01000037; GEP85657.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239UG36; -.
DR OrthoDB; 9810880at2; -.
DR Proteomes; UP000321736; Unassembled WGS sequence.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008478; F:pyridoxal 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 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:GEP85657.1};
KW Transferase {ECO:0000313|EMBL:GEP85657.1}.
FT DOMAIN 13..259
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 276 AA; 29714 MW; C3E9FF10DEFB9AA2 CRC64;
MALKKVLTIA GSDTSAGAGM QADLKTFQEL DTYGMVALAA VVTMDPKTWS HDVTPLPFEL
FNKQLETAIS IGPDAVKTGM LGSEEIIKRA GEAFTESGAK YFVVDPVMVC KGEDEVLNPG
NTDAMIKYLL PKATVTTPNL FEAGQLSGLG TLKSIDDMKK AAKIIYDQGA ENVVIKGGKA
LDQEKSYDLY YDGDKYYQLT TDMFQQSYNH GAGCTFAAAT TANLANGQSP KDAVVNAKAF
VASAIKHGWK MNDFVGPVDH GAYNRIEKID VDVKEV
//
