ID F5XGS7_MICPN Unreviewed; 284 AA.
AC F5XGS7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Pyridoxal kinase {ECO:0000313|EMBL:BAK35559.1};
DE EC=2.7.1.35 {ECO:0000313|EMBL:BAK35559.1};
GN Name=pdxY {ECO:0000313|EMBL:BAK35559.1};
GN OrderedLocusNames=MLP_25450 {ECO:0000313|EMBL:BAK35559.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK35559.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK35559.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; AP012204; BAK35559.1; -; Genomic_DNA.
DR RefSeq; WP_013863428.1; NC_015635.1.
DR AlphaFoldDB; F5XGS7; -.
DR STRING; 1032480.MLP_25450; -.
DR KEGG; mph:MLP_25450; -.
DR eggNOG; COG2240; Bacteria.
DR HOGENOM; CLU_046496_3_1_11; -.
DR OrthoDB; 9800808at2; -.
DR Proteomes; UP000007947; Chromosome.
DR GO; GO:0008478; F:pyridoxal kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR00687; pyridox_kin; 1.
DR PANTHER; PTHR10534; PYRIDOXAL KINASE; 1.
DR PANTHER; PTHR10534:SF2; PYRIDOXAL KINASE; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAK35559.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007947};
KW Transferase {ECO:0000313|EMBL:BAK35559.1}.
FT DOMAIN 94..260
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 284 AA; 30043 MW; 7ED94A86A1FA3C4A CRC64;
MTTILSIQSS VAYGHVGNSA ATFPLMRLGV EVYPVLTVHF SNHTGYPGWR GPLLAAGDVA
EVIRGIDERG ALDRVDAVLS GYQGGEDVGK VILDAVALVR SRNPRAIYCC DPVMGDVDRD
FYVRPGIPEF MRDAVVPAAQ LITPNQFELE FLTGRSTSTV PEVLAAADAA RAMGPQTVLV
TSVVHDAAQE GTIDMIAVTG EGAWSVTTPL LPQTFTGAGD LTTATFLAHL LRTDSVAEAI
GQTAATVYGV LKATVDSGES ELQLVAAQDE IAAPTRTFEV TRLR
//
