ID   PDXY_PSEF5              Reviewed;         290 AA.
AC   Q4K3F6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Pyridoxamine kinase;
DE            Short=PM kinase;
DE            EC=2.7.1.35;
GN   Name=pdxY; OrderedLocusNames=PFL_6169;
OS   Pseudomonas fluorescens (strain Pf-5 / ATCC BAA-477).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A.,
RA   Rosovitz M.J., Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W.,
RA   Nelson W.C., Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A.,
RA   Pierson L.S. III, Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas
RT   fluorescens Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
CC   -!- FUNCTION: Phosphorylates B6 vitamers; functions in a salvage
CC       pathway. Uses pyridoxamine (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyridoxal = ADP + pyridoxal 5'-
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the pyridoxine kinase family.
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DR   EMBL; CP000076; AAY95357.1; -; Genomic_DNA.
DR   RefSeq; YP_263227.1; -.
DR   GeneID; 3480539; -.
DR   GenomeReviews; CP000076_GR; PFL_6169.
DR   KEGG; pfl:PFL_6169; -.
DR   NMPDR; fig|220664.3.peg.97; -.
DR   HOGENOM; Q4K3F6; -.
DR   OMA; Q4K3F6; EVLLETQ.
DR   BioCyc; PFLU220664:PFL_6169-MON; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004340; F:glucokinase activity; IEA:HAMAP.
DR   GO; GO:0008478; F:pyridoxal kinase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01639; -; 1.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   TIGRFAMs; TIGR00687; pyridox_kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN         1    290       Pyridoxamine kinase.
FT                                /FTId=PRO_0000269819.
FT   NP_BIND     184    185       ATP (By similarity).
FT   BINDING      12     12       Substrate (By similarity).
FT   BINDING      47     47       Substrate (By similarity).
FT   BINDING     225    225       Substrate (By similarity).
SQ   SEQUENCE   290 AA;  31264 MW;  A86B14491A019730 CRC64;
     MKRTPHLLAI QSHVVFGHAG NSAAVFPMQR VGVNVWPLNT VQFSNHTQYG QWAGEVLAPQ
     QIPELVEGIA AIGELGNCDA VLSGYLGSAA QGRAILSGVA RIKAVNPKAL YLCDPVMGHP
     EKGCSVPAEV SDFLLDEAVA MADFLCPNQL ELDSFCGRKP QSLFDCLGMA RSLLDKGPRA
     VLVKHLDYPG KLVDGFEMLL VTADGSWHLR RPLLAFPRQP VGVGDLTSGL FLARVLLGDS
     LVAAFEFTAA AVHEVLLETQ ACASYELELV RAQDRIAHPR VRFEATPIGF
//