ID B7LQN4_ESCF3 Unreviewed; 286 AA.
AC B7LQN4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 30.
DE RecName: Full=Pyridoxamine kinase;
DE Short=PM kinase;
DE EC=2.7.1.35;
GN Name=pdxY; OrderedLocusNames=EFER_1407;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CU928158; CAQ88927.1; -; Genomic_DNA.
DR RefSeq; YP_002382559.1; NC_011740.1.
DR ProteinModelPortal; B7LQN4; -.
DR STRING; 585054.EFER_1407; -.
DR EnsemblBacteria; CAQ88927; CAQ88927; EFER_1407.
DR GeneID; 7123507; -.
DR KEGG; efe:EFER_1407; -.
DR PATRIC; 32127212; VBIEscFer122920_1360.
DR eggNOG; COG2240; -.
DR HOGENOM; HOG000258173; -.
DR KO; K00868; -.
DR ProtClustDB; PRK05756; -.
DR BioCyc; EFER585054:GJJM-1401-MONOMER; -.
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:0051156; P:glucose 6-phosphate metabolic process; IEA:GOC.
DR GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IEA:InterPro.
DR HAMAP; MF_01639; PdxY; 1; -.
DR InterPro; IPR013749; HMP-P_kinase-1.
DR InterPro; IPR004625; PyrdxlP_synth_PyrdxlKinase.
DR InterPro; IPR023685; Pyridoxal_kinase_PdxY.
DR PANTHER; PTHR10534; PTHR10534; 1.
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 NP_BIND 181 182 ATP (By similarity).
FT NP_BIND 207 222 ATP (By similarity).
FT BINDING 9 9 Substrate (By similarity).
FT BINDING 44 44 Substrate (By similarity).
FT BINDING 223 223 Substrate (By similarity).
SQ SEQUENCE 286 AA; 31096 MW; 218946D9DF7654FB CRC64;
MKNILAIQSH VVFGHAGNSA AEFPMRRLGA NVWPLNTVQF SNHTQYGKWT GCVMPPSHLT
EIVQGIAAIN KLQTCDAVLS GYLGSAEQGE HILGIVRQVK EANPQAKYFC DPVMGHPEKG
CIVAPGVAEF HVRYSLPASD IIAPNLVELE ILCEHPVHNV AEAVAAAREL IAKGPQIVLV
KHLARAGYSA DRFEMLLVTA DEAWHISRPL VDFGARQPVG VGDVTSGLLL VKLLQGATLQ
QALEHVTAAV YEIMLTTKAM QEYELQVVAA QDRIAKPEHY FSATQL
//
