PDXY_PSEAE
ID PDXY_PSEAE Reviewed; 288 AA.
AC Q9HT57;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Pyridoxal kinase PdxY {ECO:0000255|HAMAP-Rule:MF_01639};
DE Short=PL kinase {ECO:0000255|HAMAP-Rule:MF_01639};
DE EC=2.7.1.35 {ECO:0000255|HAMAP-Rule:MF_01639};
GN Name=pdxY {ECO:0000255|HAMAP-Rule:MF_01639}; OrderedLocusNames=PA5516;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Pyridoxal kinase involved in the salvage pathway of pyridoxal
CC 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP.
CC {ECO:0000255|HAMAP-Rule:MF_01639}.
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:0000255|HAMAP-Rule:MF_01639};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01639};
CC -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal
CC 5'-phosphate from pyridoxal: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01639}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01639}.
CC -!- SIMILARITY: Belongs to the pyridoxine kinase family. PdxY subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01639}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG08901.1; -; Genomic_DNA.
DR PIR; C82956; C82956.
DR RefSeq; NP_254203.1; NC_002516.2.
DR RefSeq; WP_003114134.1; NZ_QZGE01000012.1.
DR PDB; 5B6A; X-ray; 2.00 A; A=1-288.
DR PDBsum; 5B6A; -.
DR AlphaFoldDB; Q9HT57; -.
DR SMR; Q9HT57; -.
DR STRING; 287.DR97_2894; -.
DR PaxDb; Q9HT57; -.
DR PRIDE; Q9HT57; -.
DR DNASU; 878628; -.
DR EnsemblBacteria; AAG08901; AAG08901; PA5516.
DR GeneID; 878628; -.
DR KEGG; pae:PA5516; -.
DR PATRIC; fig|208964.12.peg.5781; -.
DR PseudoCAP; PA5516; -.
DR HOGENOM; CLU_046496_3_0_6; -.
DR InParanoid; Q9HT57; -.
DR OMA; CPNQLEL; -.
DR PhylomeDB; Q9HT57; -.
DR BioCyc; PAER208964:G1FZ6-5643-MON; -.
DR UniPathway; UPA01068; UER00298.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008478; F:pyridoxal kinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IBA:GO_Central.
DR CDD; cd01173; pyridoxal_pyridoxamine_kinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01639; PdxY; 1.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlKinase.
DR InterPro; IPR023685; Pyridoxal_kinase_PdxY.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR10534; PTHR10534; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..288
FT /note="Pyridoxal kinase PdxY"
FT /id="PRO_0000269818"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 47..48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 211..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01639"
FT STRAND 6..17
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 34..45
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 89..105
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:5B6A"
FT TURN 137..141
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 149..156
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:5B6A"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 241..262
FT /evidence="ECO:0007829|PDB:5B6A"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:5B6A"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:5B6A"
SQ SEQUENCE 288 AA; 31285 MW; 6440394E762AFF4B CRC64;
MPRTPHLLAI QSHVVFGHAG NAAAVFPMQR IGINVWPLNT VQFSNHTQYG RWTGQVLPPE
QIPALVDGIA GIGELGNCDA VLSGYLGSAA QGRAILDVVA RIKQANPRAL YLCDPVMGHP
EKGCIVAPEV SDFLLEEAAA VADYLCPNQL ELDSFCDRQP NSLADCVEMA RSLLARGPRA
ILVKHLNYPG KAGDTFEMLL VAADQAWHLQ RPLLAFPRQP VGVGDLASGL FLSRLLLGDD
LRNAFEFTGA AVHEVLLETQ ACGSYELELV RAQDRIAHPR VRFDAVRL
