YAJO_ECOLI
ID YAJO_ECOLI Reviewed; 324 AA.
AC P77735; Q2MC07;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=1-deoxyxylulose-5-phosphate synthase YajO {ECO:0000305};
DE EC=1.1.-.- {ECO:0000269|PubMed:25326299};
GN Name=yajO; OrderedLocusNames=b0419, JW0409;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP OVEREXPRESSION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15292217; DOI=10.1074/jbc.m404284200;
RA Lawhorn B.G., Gerdes S.Y., Begley T.P.;
RT "A genetic screen for the identification of thiamin metabolic genes.";
RL J. Biol. Chem. 279:43555-43559(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND OVEREXPRESSION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=25326299; DOI=10.1128/aem.02920-14;
RA Kirby J., Nishimoto M., Chow R.W., Baidoo E.E., Wang G., Martin J.,
RA Schackwitz W., Chan R., Fortman J.L., Keasling J.D.;
RT "Enhancing terpene yield from sugars via novel routes to 1-deoxy-d-xylulose
RT 5-phosphate.";
RL Appl. Environ. Microbiol. 81:130-138(2015).
CC -!- FUNCTION: Catalyzes the conversion of ribulose 5-phosphate (Ru5P) to 1-
CC deoxy-D-xylulose 5-phosphate (DXP), providing a direct route from
CC pentoses to terpenes. May play a role in biosynthesis of DXP under
CC conditions of thiamine starvation. {ECO:0000269|PubMed:25326299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + D-ribulose 5-phosphate = 1-deoxy-D-xylulose 5-phosphate
CC + A + H2O; Xref=Rhea:RHEA:56944, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:58121; Evidence={ECO:0000269|PubMed:25326299};
CC -!- ACTIVITY REGULATION: NADH, NADPH or ATP do not increase activity.
CC {ECO:0000269|PubMed:25326299}.
CC -!- MISCELLANEOUS: Overexpression supports cell viability in the absence of
CC the essential dxs-encoded 1-deoxy-D-xylulose-5-phosphate synthase
CC (PubMed:25326299). Overexpression confers resistance to the 4-amino-2-
CC methyl 5-hydroxymethylpyrimidine (HMP) analogs bacimethrin and 4-amino-
CC 2-trifluoromethyl 5-hydroxymethylpyrimidine (CF(3)-HMP)
CC (PubMed:15292217). {ECO:0000269|PubMed:15292217,
CC ECO:0000269|PubMed:25326299}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40175.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U82664; AAB40175.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73522.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76199.1; -; Genomic_DNA.
DR PIR; C64771; C64771.
DR RefSeq; NP_414953.2; NC_000913.3.
DR RefSeq; WP_001199800.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P77735; -.
DR SMR; P77735; -.
DR BioGRID; 4259835; 111.
DR DIP; DIP-11291N; -.
DR IntAct; P77735; 6.
DR STRING; 511145.b0419; -.
DR TCDB; 8.A.5.1.6; the voltage-gated k(+) channel Beta-subunit (kvBeta) family.
DR jPOST; P77735; -.
DR PaxDb; P77735; -.
DR PRIDE; P77735; -.
DR EnsemblBacteria; AAC73522; AAC73522; b0419.
DR EnsemblBacteria; BAE76199; BAE76199; BAE76199.
DR GeneID; 946903; -.
DR KEGG; ecj:JW0409; -.
DR KEGG; eco:b0419; -.
DR PATRIC; fig|1411691.4.peg.1858; -.
DR EchoBASE; EB3377; -.
DR eggNOG; COG0667; Bacteria.
DR HOGENOM; CLU_023205_2_0_6; -.
DR InParanoid; P77735; -.
DR OMA; VDLWQVH; -.
DR PhylomeDB; P77735; -.
DR BioCyc; EcoCyc:G6236-MON; -.
DR BioCyc; MetaCyc:G6236-MON; -.
DR BRENDA; 2.2.1.7; 2026.
DR PRO; PR:P77735; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006772; P:thiamine metabolic process; EXP:EcoliWiki.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..324
FT /note="1-deoxyxylulose-5-phosphate synthase YajO"
FT /id="PRO_0000070392"
FT ACT_SITE 61
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CG76"
SQ SEQUENCE 324 AA; 36420 MW; 0B69E09F2BEDF9B1 CRC64;
MQYNPLGKTD LRVSRLCLGC MTFGEPDRGN HAWTLPEESS RPIIKRALEG GINFFDTANS
YSDGSSEEIV GRALRDFARR EDVVVATKVF HRVGDLPEGL SRAQILRSID DSLRRLGMDY
VDILQIHRWD YNTPIEETLE ALNDVVKAGK ARYIGASSMH ASQFAQALEL QKQHGWAQFV
SMQDHYNLIY REEEREMLPL CYQEGVAVIP WSPLARGRLT RPWGETTARL VSDEVGKNLY
KESDENDAQI AERLTGVSEE LGATRAQVAL AWLLSKPGIA APIIGTSREE QLDELLNAVD
ITLKPEQIAE LETPYKPHPV VGFK
