ID   PDXY_PSE14              Reviewed;         288 AA.
AC   Q48BL6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Pyridoxamine kinase;
DE            Short=PM kinase;
DE            EC=2.7.1.35;
GN   Name=pdxY; OrderedLocusNames=PSPPH_5152;
OS   Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=264730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA   Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA   Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L.,
RA   Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O.,
RA   Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D.,
RA   Mansfield J.W., Collmer A., Buell R.;
RT   "Whole-genome sequence analysis of Pseudomonas syringae pv.
RT   phaseolicola 1448A reveals divergence among pathovars in genes
RT   involved in virulence and transposition.";
RL   J. Bacteriol. 187:6488-6498(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; CP000058; AAZ36132.1; -; Genomic_DNA.
DR   RefSeq; YP_277229.1; -.
DR   GeneID; 3558742; -.
DR   GenomeReviews; CP000058_GR; PSPPH_5152.
DR   KEGG; psp:PSPPH_5152; -.
DR   NMPDR; fig|264730.3.peg.5169; -.
DR   HOGENOM; Q48BL6; -.
DR   OMA; Q48BL6; EVLLETQ.
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; IPR011611; Carb/pur_kinase.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   Pfam; PF00294; PfkB; 1.
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    288       Pyridoxamine kinase.
FT                                /FTId=PRO_0000269822.
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   288 AA;  31012 MW;  67295C04ED48F0F7 CRC64;
     MKRTPHLLAI QSHVVFGHAG NSAAVFPMQR IGVNVWPLNT VQFSNHTQYK QWTGEVLAPQ
     QIPALIEGIA AIGELGNCDA VLSGYLGSAA QGRAILTGVA RIKAANPKAL YLCDPVMGHP
     EKGCIVAPEV SDFLLQEAAA MADFMCPNQL ELDSFSGRKP ESLADCLAMA RALLARGPKA
     VVVKHLDYPG KAADGFEMLL VTAEASWHLR RPLLAFPRQP VGVGDLTSGL FLSRILLGDD
     LVAAFEFTAA AVHEVLLETQ ACGSYELELV RAQDRIAHPR VKFDAVRL
//