PDXI_ECOLI
ID PDXI_ECOLI Reviewed; 286 AA.
AC P25906;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Pyridoxine 4-dehydrogenase {ECO:0000303|PubMed:27941785};
DE EC=1.1.1.65 {ECO:0000269|PubMed:27941785};
GN Name=pdxI {ECO:0000303|PubMed:27941785};
GN Synonyms=ydbC {ECO:0000312|EMBL:AAC74488.1};
GN OrderedLocusNames=b1406, JW1403;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1665988; DOI=10.1016/0300-9084(91)90166-x;
RA Moszer I., Glaser P., Danchin A.;
RT "Multiple IS insertion sequences near the replication terminus in
RT Escherichia coli K-12.";
RL Biochimie 73:1361-1374(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=9748275; DOI=10.1074/jbc.273.40.25974;
RA Ferrandez A., Minambres B., Garcia B., Olivera E.R., Luengo J.M.,
RA Garcia J.L., Diaz E.;
RT "Catabolism of phenylacetic acid in Escherichia coli. Characterization of a
RT new aerobic hybrid pathway.";
RL J. Biol. Chem. 273:25974-25986(1998).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21332126; DOI=10.1021/bi101763c;
RA Khersonsky O., Malitsky S., Rogachev I., Tawfik D.S.;
RT "Role of chemistry versus substrate binding in recruiting promiscuous
RT enzyme functions.";
RL Biochemistry 50:2683-2690(2011).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=27941785; DOI=10.1038/nmeth.4103;
RA Sevin D.C., Fuhrer T., Zamboni N., Sauer U.;
RT "Nontargeted in vitro metabolomics for high-throughput identification of
RT novel enzymes in Escherichia coli.";
RL Nat. Methods 14:187-194(2017).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of pyridoxal to
CC pyridoxine in vitro. Is not able to reduce 4-pyridoxate, and to oxidize
CC pyridoxine or pyridoxamine (PubMed:27941785). Has Kemp eliminase
CC activity towards the non-physiological substrate 5-nitrobenzisoxazole,
CC producing 4-nitro-2-cyanophenol; this activity is not considered to be
CC physiologically relevant (PubMed:21332126).
CC {ECO:0000269|PubMed:21332126, ECO:0000269|PubMed:27941785}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal;
CC Xref=Rhea:RHEA:16129, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:17310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.65;
CC Evidence={ECO:0000269|PubMed:27941785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + pyridoxine = H(+) + NADH + pyridoxal;
CC Xref=Rhea:RHEA:52684, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:17310, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:27941785};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=270 uM for 5-nitrobenzisoxazole {ECO:0000269|PubMed:21332126};
CC Note=kcat is 0.11 sec(-1) for the Kemp eliminase activity towards 5-
CC nitrobenzisoxazole. {ECO:0000269|PubMed:21332126};
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
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DR EMBL; X62680; CAA44553.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74488.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15021.1; -; Genomic_DNA.
DR EMBL; X97452; CAA66103.1; -; Genomic_DNA.
DR PIR; A48399; A48399.
DR RefSeq; NP_415924.1; NC_000913.3.
DR RefSeq; WP_000097801.1; NZ_SSZK01000021.1.
DR AlphaFoldDB; P25906; -.
DR SMR; P25906; -.
DR BioGRID; 4263019; 15.
DR DIP; DIP-11632N; -.
DR IntAct; P25906; 4.
DR STRING; 511145.b1406; -.
DR SWISS-2DPAGE; P25906; -.
DR jPOST; P25906; -.
DR PaxDb; P25906; -.
DR PRIDE; P25906; -.
DR DNASU; 945980; -.
DR EnsemblBacteria; AAC74488; AAC74488; b1406.
DR EnsemblBacteria; BAA15021; BAA15021; BAA15021.
DR GeneID; 66674742; -.
DR GeneID; 945980; -.
DR KEGG; ecj:JW1403; -.
DR KEGG; eco:b1406; -.
DR PATRIC; fig|1411691.4.peg.865; -.
DR EchoBASE; EB1285; -.
DR eggNOG; COG0667; Bacteria.
DR HOGENOM; CLU_023205_2_1_6; -.
DR InParanoid; P25906; -.
DR OMA; GYGTMQL; -.
DR PhylomeDB; P25906; -.
DR BioCyc; EcoCyc:EG11309-MON; -.
DR BioCyc; MetaCyc:EG11309-MON; -.
DR PRO; PR:P25906; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR GO; GO:0050236; F:pyridoxine:NADP 4-dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0009443; P:pyridoxal 5'-phosphate salvage; IMP:EcoCyc.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..286
FT /note="Pyridoxine 4-dehydrogenase"
FT /id="PRO_0000070393"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 210..218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 30706 MW; 82B587AEA9115EF9 CRC64;
MSSNTFTLGT KSVNRLGYGA MQLAGPGVFG PPRDRHVAIT VLREALALGV NHIDTSDFYG
PHVTNQIIRE ALYPYSDDLT IVTKIGARRG EDASWLPAFS PAELQKAVHD NLRNLGLDVL
DVVNLRVMMG DGHGPAEGSI EASLTVLAEM QQQGLVKHIG LSNVTPTQVA EARKIAEIVC
VQNEYNIAHR ADDAMIDALA HDGIAYVPFF PLGGFTPLQS STLSDVAASL GATPMQVALA
WLLQRSPNIL LIPGTSSVAH LRENMAAEKL HLSEEVLSTL DGISRE
