ID W9G2X3_9MICO Unreviewed; 282 AA.
AC W9G2X3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Pyridoxamine kinase {ECO:0000313|EMBL:EWS99631.1};
GN ORFNames=N865_21765 {ECO:0000313|EMBL:EWS99631.1};
OS Intrasporangium oryzae NRRL B-24470.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWS99631.1, ECO:0000313|Proteomes:UP000019489};
RN [1] {ECO:0000313|EMBL:EWS99631.1, ECO:0000313|Proteomes:UP000019489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWS99631.1,
RC ECO:0000313|Proteomes:UP000019489};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) 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};
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:EWS99631.1}.
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DR EMBL; AWSA01000085; EWS99631.1; -; Genomic_DNA.
DR RefSeq; WP_034810203.1; NZ_AWSA01000085.1.
DR AlphaFoldDB; W9G2X3; -.
DR STRING; 1386089.N865_21765; -.
DR PATRIC; fig|1386089.3.peg.4155; -.
DR eggNOG; COG2240; Bacteria.
DR OrthoDB; 9800808at2; -.
DR Proteomes; UP000019489; Unassembled WGS sequence.
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:EWS99631.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019489};
KW Transferase {ECO:0000313|EMBL:EWS99631.1}.
FT DOMAIN 92..250
FT /note="Pyridoxamine kinase/Phosphomethylpyrimidine kinase"
FT /evidence="ECO:0000259|Pfam:PF08543"
SQ SEQUENCE 282 AA; 29747 MW; 8ED9C9E4B1EEE645 CRC64;
MKILSIQSHV AYGHAGNSAA VFPLQRLGHD VYPVLTVTFS NHTGYGATRG PLIAPTDVAE
VLLGVEERGA FPSIDAVLSG YQGAEAVGQV VLDAVARVKA ANPAAIYCCD PVMGDVGRGF
FVREGIPEYL RDEVVPRADI VTPNQFELEF LVGRTVGTLS ELVAAADELR ARGPECVLVT
SALTSDTPDG SIQMACVTGE GAWVVTTPML PMTVRGGGDV TAAVFLAHYL TDGAQEALKR
TAATMYSILE RTHASGSEEM LLVAEQEAIA NPQTVFEVSA VR
//
