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Database: UniProt
Entry: A0A2W2CMH7_9ACTN
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ID   A0A2W2CMH7_9ACTN        Unreviewed;       283 AA.
AC   A0A2W2CMH7;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pyridoxal kinase {ECO:0000313|EMBL:BCJ57561.1, ECO:0000313|EMBL:PZG00712.1};
GN   Name=pdxY {ECO:0000313|EMBL:BCJ57561.1};
GN   ORFNames=C1I93_01610 {ECO:0000313|EMBL:PZG00712.1}, Jiend_09830
GN   {ECO:0000313|EMBL:BCJ57561.1};
OS   Micromonospora endophytica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=515350 {ECO:0000313|EMBL:PZG00712.1, ECO:0000313|Proteomes:UP000248627};
RN   [1] {ECO:0000313|EMBL:PZG00712.1, ECO:0000313|Proteomes:UP000248627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45430 {ECO:0000313|EMBL:PZG00712.1,
RC   ECO:0000313|Proteomes:UP000248627};
RA   Sahin N., Ay H., Saygin H.;
RT   "Draft genome sequence of Jishengella endophytica.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BCJ57561.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 109090 {ECO:0000313|EMBL:BCJ57561.1};
RA   Komaki H., Tamura T.;
RT   "Whole genome shotgun sequence of Jishengella endophytica NBRC 109090.";
RL   Submitted (AUG-2020) 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; AP023358; BCJ57561.1; -; Genomic_DNA.
DR   EMBL; POTX01000005; PZG00712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W2CMH7; -.
DR   KEGG; meno:Jiend_09830; -.
DR   OrthoDB; 9800808at2; -.
DR   Proteomes; UP000248627; Unassembled WGS sequence.
DR   Proteomes; UP000682317; 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:PZG00712.1};
KW   Transferase {ECO:0000313|EMBL:PZG00712.1}.
FT   DOMAIN          102..258
FT                   /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF08543"
SQ   SEQUENCE   283 AA;  29563 MW;  BDFC5842A910BAE2 CRC64;
     MRILSIQSSV AYGHVGNSAA VFPLQRLGHE VWPVLTVHFS NHTGYGAWRG PLLAPADVAE
     VIAGIADRGV LGDADAVLSG YQGDPAMGAV ILDAVTLVKT ANPAAVYCCD PVMGDVGRGI
     FVRPGIPEYL RDVVVPRADI ITPNHFELDF LAGRTTNSLA EVLAAVDVVR ATGPRHVLVT
     SVLHEEVPPG SLEVVAVSDE GAWAVTTPLL PINPNGGGDV TAALYLAHLA TSGSPARALE
     RTVAAVFTVL EATLAAGTRE IQLIAAQDAI ADPPIRFAAR RLR
//
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