ID   PDXY_HAES1              Reviewed;         286 AA.
AC   Q0I3D2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Pyridoxamine kinase;
DE            Short=PM kinase;
DE            EC=2.7.1.35;
GN   Name=pdxY; OrderedLocusNames=HS_0933;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17172329; DOI=10.1128/JB.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni)
RT   strain 129Pt and comparison to Haemophilus ducreyi 35000HP and
RT   Haemophilus influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
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; CP000436; ABI25208.1; -; Genomic_DNA.
DR   RefSeq; YP_719144.1; -.
DR   GeneID; 4240426; -.
DR   GenomeReviews; CP000436_GR; HS_0933.
DR   KEGG; hso:HS_0933; -.
DR   NMPDR; fig|205914.1.peg.1082; -.
DR   HOGENOM; Q0I3D2; -.
DR   OMA; Q0I3D2; EVLLETQ.
DR   BioCyc; HSOM205914:HS_0933-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; IPR013749; HMP-P_kinase-1.
DR   InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR   Pfam; PF08543; Phos_pyr_kin; 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    286       Pyridoxamine kinase.
FT                                /FTId=PRO_0000269812.
FT   NP_BIND     181    182       ATP (By similarity).
FT   BINDING       9      9       Substrate (By similarity).
FT   BINDING      44     44       Substrate (By similarity).
FT   BINDING     222    222       Substrate (By similarity).
SQ   SEQUENCE   286 AA;  31347 MW;  1846ACBCAC5A3ECC CRC64;
     MKNILSIQSH VVYGYAGNKS ATFPMQLLGI DVWALNTVQF SNHTQYGKWT GMVIPKEQIG
     EIVQGIDNIG ELHQCDAVLS GYIGSAEQVE EIIKAFHKIK ERNPKAIYLC DPVMGHPDKG
     CVVADGVKEG LIKIAMAQAD IITPNLVELR ELSGLAVENF EQAIEAVKVI LSKGPKKVLV
     KHLSRVGKNA AQFEMLLANN DGIWHISRPL HNFNKEPVGV GDLTAGLFLA NLLNGKSDVE
     AFEHTANTVN DVMETTHNAG VYELQTIAAR EWIVNPKSQY KAVKIG
//