AKRMG_ECOLI
ID AKRMG_ECOLI Reviewed; 326 AA.
AC P77256;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=NADH-specific methylglyoxal reductase {ECO:0000303|PubMed:16813561};
DE EC=1.1.1.- {ECO:0000269|PubMed:16813561};
DE AltName: Full=AKR11B2 {ECO:0000303|PubMed:16813561};
GN Name=ydjG; OrderedLocusNames=b1771, JW1760;
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 / 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 [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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, SUBUNIT, MUTAGENESIS OF ASP-232, AND 3D-STRUCTURE MODELING.
RX PubMed=16813561; DOI=10.1042/bj20060660;
RA Di Luccio E., Elling R.A., Wilson D.K.;
RT "Identification of a novel NADH-specific aldo-keto reductase using sequence
RT and structural homologies.";
RL Biochem. J. 400:105-114(2006).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=20562286; DOI=10.1128/aem.00242-10;
RA Vogel-Scheel J., Alpert C., Engst W., Loh G., Blaut M.;
RT "Requirement of purine and pyrimidine synthesis for colonization of the
RT mouse intestine by Escherichia coli.";
RL Appl. Environ. Microbiol. 76:5181-5187(2010).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=22074179; DOI=10.1186/1475-2859-10-97;
RA Jain R., Yan Y.;
RT "Dehydratase mediated 1-propanol production in metabolically engineered
RT Escherichia coli.";
RL Microb. Cell Fact. 10:97-97(2011).
CC -!- FUNCTION: Catalyzes the NADH-dependent reduction of methylglyoxal (2-
CC oxopropanal) in vitro (PubMed:16813561). It is not known if this
CC activity has physiological significance (PubMed:16813561). Cannot use
CC NADPH as a cosubstrate (PubMed:16813561). Seems to play some role in
CC intestinal colonization (PubMed:20562286).
CC {ECO:0000269|PubMed:16813561, ECO:0000269|PubMed:20562286}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydroxyacetone + NAD(+) = H(+) + methylglyoxal + NADH;
CC Xref=Rhea:RHEA:35615, ChEBI:CHEBI:15378, ChEBI:CHEBI:17158,
CC ChEBI:CHEBI:27957, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:16813561};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52 uM for NADH {ECO:0000269|PubMed:16813561};
CC KM=1.81 mM for methylglyoxal {ECO:0000269|PubMed:16813561};
CC KM=363 mM for DL-glyceraldehyde {ECO:0000269|PubMed:16813561};
CC Note=kcat is 15.7 sec(-1) with methylglyoxal as substrate. kcat is 2
CC sec(-1) with DL-glyceraldehyde as substrate.
CC {ECO:0000269|PubMed:16813561};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16813561}.
CC -!- INDUCTION: Is 3.5-fold up-regulated in vivo in intestinal environment
CC compared to the level for in vitro cultures.
CC {ECO:0000269|PubMed:20562286}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene affects intestinal
CC colonization by E.coli, since a deletion mutant reaches a 1.2-log-lower
CC cecal concentration than the wild-type. {ECO:0000269|PubMed:20562286}.
CC -!- BIOTECHNOLOGY: Can be used in an engineered metabolic pathway for 1,2-
CC propanediol and 1-propanol production. 1-propanol is a potential fuel
CC substitute to petroleum. {ECO:0000269|PubMed:22074179}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC reductase 11 subfamily. {ECO:0000305|PubMed:16813561}.
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DR EMBL; U00096; AAC74841.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15562.1; -; Genomic_DNA.
DR PIR; C64937; C64937.
DR RefSeq; NP_416285.1; NC_000913.3.
DR RefSeq; WP_000723710.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P77256; -.
DR SMR; P77256; -.
DR BioGRID; 4259143; 11.
DR IntAct; P77256; 3.
DR STRING; 511145.b1771; -.
DR PaxDb; P77256; -.
DR PRIDE; P77256; -.
DR EnsemblBacteria; AAC74841; AAC74841; b1771.
DR EnsemblBacteria; BAA15562; BAA15562; BAA15562.
DR GeneID; 946283; -.
DR KEGG; ecj:JW1760; -.
DR KEGG; eco:b1771; -.
DR PATRIC; fig|1411691.4.peg.483; -.
DR EchoBASE; EB3256; -.
DR eggNOG; COG0667; Bacteria.
DR HOGENOM; CLU_023205_2_3_6; -.
DR InParanoid; P77256; -.
DR OMA; FGCSTFP; -.
DR PhylomeDB; P77256; -.
DR BioCyc; EcoCyc:G6958-MON; -.
DR BioCyc; MetaCyc:G6958-MON; -.
DR SABIO-RK; P77256; -.
DR PRO; PR:P77256; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0103030; F:ethylglyoxal reductase (NADH-dependent, hydroxyacetone-forming) activity; IEA:RHEA.
DR GO; GO:0019170; F:methylglyoxal reductase (NADH-dependent) activity; IDA:EcoCyc.
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 NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..326
FT /note="NADH-specific methylglyoxal reductase"
FT /id="PRO_0000070395"
FT ACT_SITE 59
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT BINDING 20..21
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT BINDING 54
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT BINDING 217..222
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT BINDING 291
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT BINDING 297
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT SITE 85
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P80874"
FT MUTAGEN 232
FT /note="D->A,E: Converts the protein into an enzyme with
FT dual specificity, i.e. that is able to use both NADPH and
FT NADH as cosubstrates."
FT /evidence="ECO:0000269|PubMed:16813561"
SQ SEQUENCE 326 AA; 36329 MW; 1FF5C52522708978 CRC64;
MKKIPLGTTD ITLSRMGLGT WAIGGGPAWN GDLDRQICID TILEAHRCGI NLIDTAPGYN
FGNSEVIVGQ ALKKLPREQV VVETKCGIVW ERKGSLFNKV GDRQLYKNLS PESIREEVAA
SLQRLGIDYI DIYMTHWQSV PPFFTPIAET VAVLNELKSE GKIRAIGAAN VDADHIREYL
QYGELDIIQA KYSILDRAME NELLPLCRDN GIVVQVYSPL EQGLLTGTIT RDYVPGGARA
NKVWFQRENM LKVIDMLEQW QPLCARYQCT IPTLALAWIL KQSDLISILS GATAPEQVRE
NVAALNINLS DADATLMREM AEALER
