ALDA_ECOLI
ID ALDA_ECOLI Reviewed; 479 AA.
AC P25553;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Lactaldehyde dehydrogenase {ECO:0000303|PubMed:6345530};
DE EC=1.2.1.22 {ECO:0000269|PubMed:27671251, ECO:0000269|PubMed:3298215, ECO:0000269|PubMed:3308886, ECO:0000269|PubMed:6345530};
DE AltName: Full=Aldehyde dehydrogenase A;
DE AltName: Full=Glycolaldehyde dehydrogenase {ECO:0000303|PubMed:6345530};
DE EC=1.2.1.21 {ECO:0000269|PubMed:16731973, ECO:0000269|PubMed:31850327, ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3308886, ECO:0000269|PubMed:6345530};
GN Name=aldA; Synonyms=ald {ECO:0000303|PubMed:3298215};
GN OrderedLocusNames=b1415, JW1412;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC STRAIN=K12;
RX PubMed=1917845; DOI=10.1128/jb.173.19.6118-6123.1991;
RA Hidalgo E., Chen Y.-M., Lin E.C.C., Aguilar J.;
RT "Molecular cloning and DNA sequencing of the Escherichia coli K-12 ald gene
RT encoding aldehyde dehydrogenase.";
RL J. Bacteriol. 173:6118-6123(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 PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=6345530; DOI=10.1016/s0021-9258(18)32248-8;
RA Caballero E., Baldoma L., Ros J., Boronat A., Aguilar J.;
RT "Identification of lactaldehyde dehydrogenase and glycolaldehyde
RT dehydrogenase as functions of the same protein in Escherichia coli.";
RL J. Biol. Chem. 258:7788-7792(1983).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=3298215; DOI=10.1128/jb.169.7.3289-3294.1987;
RA Chen Y.M., Zhu Y., Lin E.C.;
RT "NAD-linked aldehyde dehydrogenase for aerobic utilization of L-fucose and
RT L-rhamnose by Escherichia coli.";
RL J. Bacteriol. 169:3289-3294(1987).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=3308886; DOI=10.1016/s0021-9258(18)47893-3;
RA Baldoma L., Aguilar J.;
RT "Involvement of lactaldehyde dehydrogenase in several metabolic pathways of
RT Escherichia coli K12.";
RL J. Biol. Chem. 262:13991-13996(1987).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=3275622; DOI=10.1128/jb.170.1.416-421.1988;
RA Baldoma L., Aguilar J.;
RT "Metabolism of L-fucose and L-rhamnose in Escherichia coli: aerobic-
RT anaerobic regulation of L-lactaldehyde dissimilation.";
RL J. Bacteriol. 170:416-421(1988).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16731973; DOI=10.1110/ps.052039606;
RA Rodriguez-Zavala J.S., Allali-Hassani A., Weiner H.;
RT "Characterization of E. coli tetrameric aldehyde dehydrogenases with
RT atypical properties compared to other aldehyde dehydrogenases.";
RL Protein Sci. 15:1387-1396(2006).
RN [11]
RP MUTAGENESIS OF PHE-180.
RX PubMed=18218709; DOI=10.1110/ps.073277108;
RA Rodriguez-Zavala J.S.;
RT "Enhancement of coenzyme binding by a single point mutation at the coenzyme
RT binding domain of E. coli lactaldehyde dehydrogenase.";
RL Protein Sci. 17:563-570(2008).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASN-286.
RX PubMed=27671251; DOI=10.1080/09168451.2016.1194181;
RA Wu X., Xu L., Yan M.;
RT "A new NAD+-dependent glyceraldehyde dehydrogenase obtained by rational
RT design of L-lactaldehyde dehydrogenase from Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 80:2306-2310(2016).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31850327; DOI=10.3389/fbioe.2019.00359;
RA Lachaux C., Frazao C.J.R., Kraubetaer F., Morin N., Walther T.,
RA Francois J.M.;
RT "A new synthetic pathway for the bioproduction of glycolic acid from
RT lignocellulosic sugars aimed at maximal carbon conservation.";
RL Front. Bioeng. Biotechnol. 7:359-359(2019).
RN [14] {ECO:0007744|PDB:2HG2, ECO:0007744|PDB:2ILU, ECO:0007744|PDB:2IMP}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP LACTATE; NAD AND NADP, SUBUNIT, AND ACTIVE SITE.
RX PubMed=17173928; DOI=10.1016/j.jmb.2006.11.023;
RA Di Costanzo L., Gomez G.A., Christianson D.W.;
RT "Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and
RT inferences regarding substrate and cofactor specificity.";
RL J. Mol. Biol. 366:481-493(2007).
RN [15] {ECO:0007744|PDB:2OPX}
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS).
RA Francuski D., Rossocha M., Saenger W.;
RT "Crystal structure of lactaldehyde dehydrogenase from Escherichia coli.";
RL Submitted (JAN-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the irreversible oxidation of L-lactaldehyde to L-
CC lactate (PubMed:6345530, PubMed:3298215, PubMed:3308886,
CC PubMed:27671251). Also shows high activity with glycolaldehyde and L-
CC glyceraldehyde (PubMed:6345530, PubMed:3308886, PubMed:3275622,
CC PubMed:16731973, PubMed:31850327). Has weaker activity with various
CC aldehydes such as methylglyoxal, propionaldehyde or benzaldehyde
CC (PubMed:3308886, PubMed:16731973). Involved in the degradation of
CC lactaldehyde produced during metabolism of L-fucose and L-rhamnose
CC (PubMed:3298215, PubMed:3275622). It may be involved in several other
CC metabolic pathways (PubMed:3308886). {ECO:0000269|PubMed:16731973,
CC ECO:0000269|PubMed:27671251, ECO:0000269|PubMed:31850327,
CC ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3298215,
CC ECO:0000269|PubMed:3308886, ECO:0000269|PubMed:6345530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-lactaldehyde + H2O + NAD(+) = (S)-lactate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:14277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16651, ChEBI:CHEBI:18041, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.22;
CC Evidence={ECO:0000269|PubMed:27671251, ECO:0000269|PubMed:3298215,
CC ECO:0000269|PubMed:3308886, ECO:0000269|PubMed:6345530};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14278;
CC Evidence={ECO:0000269|PubMed:3298215, ECO:0000269|PubMed:3308886};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycolaldehyde + H2O + NAD(+) = glycolate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:20001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:29805, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.21;
CC Evidence={ECO:0000269|PubMed:16731973, ECO:0000269|PubMed:31850327,
CC ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3308886,
CC ECO:0000269|PubMed:6345530};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20002;
CC Evidence={ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3308886};
CC -!- ACTIVITY REGULATION: Substrate inhibition is very strong with
CC lactaldehyde, diminishing progressively with glycolaldehyde,
CC glyceraldehyde or methylglyoxal (PubMed:3308886). Inhibited by p-
CC hydroxy mercuribenzoate and by some cations, including Mn(2+), Ca(2+),
CC Cu(2+) and Zn(2+) (PubMed:3308886). Inhibited by NADH (PubMed:3275622).
CC {ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3308886}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.04 mM for L-lactaldehyde {ECO:0000269|PubMed:3308886};
CC KM=14.5 mM for L-lactaldehyde {ECO:0000269|PubMed:27671251};
CC KM=0.38 mM for glycolaldehyde {ECO:0000269|PubMed:3308886};
CC KM=0.14 mM for glycolaldehyde {ECO:0000269|PubMed:16731973};
CC KM=0.21 mM for glycolaldehyde {ECO:0000269|PubMed:31850327};
CC KM=0.15 mM for L-glyceraldehyde {ECO:0000269|PubMed:3308886};
CC KM=1.0 mM for methylglyoxal {ECO:0000269|PubMed:3308886};
CC KM=15.2 mM for acetaldehyde {ECO:0000269|PubMed:16731973};
CC KM=0.24 mM for propionaldehyde {ECO:0000269|PubMed:16731973};
CC KM=0.15 mM for benzaldehyde {ECO:0000269|PubMed:16731973};
CC KM=4.5 mM for phenylacetaldehyde {ECO:0000269|PubMed:16731973};
CC KM=0.12 mM for NAD (in the presence of L-lactaldehyde)
CC {ECO:0000269|PubMed:3308886};
CC KM=0.28 mM for NAD (in the presence of glycolaldehyde)
CC {ECO:0000269|PubMed:3308886};
CC KM=0.038 mM for NAD (in the presence of propionaldehyde)
CC {ECO:0000269|PubMed:16731973};
CC KM=6.25 mM for NADP {ECO:0000269|PubMed:3308886};
CC Vmax=1.66 umol/min/mg enzyme with glycolaldehyde as substrate
CC {ECO:0000269|PubMed:31850327};
CC Note=kcat is 761 sec(-1) with L-lactaldehyde as substrate
CC (PubMed:27671251). kcat is 52 sec(-1) with glycolaldehyde as
CC substrate (PubMed:31850327). kcat is 1100 min(-1) with glycolaldehyde
CC as substrate. kcat is 37 min(-1) with acetaldehyde as substrate. kcat
CC is 108 min(-1) with propionaldehyde as substrate. kcat is 55 min(-1)
CC with benzaldehyde as substrate. kcat is 28 min(-1) with
CC phenylacetaldehyde as substrate (PubMed:16731973).
CC {ECO:0000269|PubMed:16731973, ECO:0000269|PubMed:27671251,
CC ECO:0000269|PubMed:31850327};
CC pH dependence:
CC Optimum pH is 10. {ECO:0000269|PubMed:27671251};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:27671251};
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation.
CC {ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3298215}.
CC -!- PATHWAY: Carbohydrate degradation; L-rhamnose degradation.
CC {ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3298215}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16731973,
CC ECO:0000269|PubMed:17173928, ECO:0000269|PubMed:3308886}.
CC -!- INDUCTION: Induced, under aerobic conditions, by at least three
CC different types of molecules, the sugars fucose and rhamnose, the diol
CC ethylene glycol and the amino acid glutamate.
CC {ECO:0000269|PubMed:3275622, ECO:0000269|PubMed:3308886,
CC ECO:0000269|PubMed:6345530}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M64541; AAA23427.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74497.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15032.1; -; Genomic_DNA.
DR PIR; A38165; A38165.
DR RefSeq; NP_415933.1; NC_000913.3.
DR RefSeq; WP_000115943.1; NZ_SSZK01000021.1.
DR PDB; 2HG2; X-ray; 2.20 A; A=1-479.
DR PDB; 2ILU; X-ray; 2.70 A; A=1-479.
DR PDB; 2IMP; X-ray; 2.10 A; A=1-479.
DR PDB; 2OPX; X-ray; 2.53 A; A=1-479.
DR PDBsum; 2HG2; -.
DR PDBsum; 2ILU; -.
DR PDBsum; 2IMP; -.
DR PDBsum; 2OPX; -.
DR AlphaFoldDB; P25553; -.
DR SMR; P25553; -.
DR BioGRID; 4260173; 13.
DR BioGRID; 850044; 1.
DR DIP; DIP-9081N; -.
DR IntAct; P25553; 5.
DR STRING; 511145.b1415; -.
DR DrugBank; DB03619; Deoxycholic acid.
DR SWISS-2DPAGE; P25553; -.
DR jPOST; P25553; -.
DR PaxDb; P25553; -.
DR PRIDE; P25553; -.
DR EnsemblBacteria; AAC74497; AAC74497; b1415.
DR EnsemblBacteria; BAA15032; BAA15032; BAA15032.
DR GeneID; 945672; -.
DR KEGG; ecj:JW1412; -.
DR KEGG; eco:b1415; -.
DR PATRIC; fig|1411691.4.peg.856; -.
DR EchoBASE; EB0034; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_5_1_6; -.
DR InParanoid; P25553; -.
DR OMA; GDHTSYV; -.
DR PhylomeDB; P25553; -.
DR BioCyc; EcoCyc:LACTALDDEHYDROG-MON; -.
DR BioCyc; MetaCyc:LACTALDDEHYDROG-MON; -.
DR BRENDA; 1.2.1.22; 2026.
DR BRENDA; 1.2.1.89; 2026.
DR SABIO-RK; P25553; -.
DR UniPathway; UPA00541; -.
DR UniPathway; UPA00563; -.
DR EvolutionaryTrace; P25553; -.
DR PRO; PR:P25553; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0050569; F:glycolaldehyde dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; ISS:EcoCyc.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR GO; GO:0042355; P:L-fucose catabolic process; IEP:EcoCyc.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0019301; P:rhamnose catabolic process; IMP:EcoCyc.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1917845,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..479
FT /note="Lactaldehyde dehydrogenase"
FT /id="PRO_0000056564"
FT ACT_SITE 251
FT /evidence="ECO:0000305|PubMed:17173928"
FT ACT_SITE 285
FT /evidence="ECO:0000305|PubMed:17173928"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 161
FT /ligand="(S)-lactate"
FT /ligand_id="ChEBI:CHEBI:16651"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 176..179
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 214
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 251
FT /ligand="(S)-lactate"
FT /ligand_id="ChEBI:CHEBI:16651"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 286
FT /ligand="(S)-lactate"
FT /ligand_id="ChEBI:CHEBI:16651"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 336
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 443
FT /ligand="(S)-lactate"
FT /ligand_id="ChEBI:CHEBI:16651"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT BINDING 449
FT /ligand="(S)-lactate"
FT /ligand_id="ChEBI:CHEBI:16651"
FT /evidence="ECO:0000269|PubMed:17173928,
FT ECO:0007744|PDB:2IMP"
FT SITE 286
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:27671251"
FT MUTAGEN 180
FT /note="F->T: Can bind and use NADP(+) as coenzyme. 16-fold
FT increase in catalytic efficiency with NAD(+) as coenzyme."
FT /evidence="ECO:0000269|PubMed:18218709"
FT MUTAGEN 286
FT /note="N->E: 4-fold increase in catalytic efficiency with
FT L-lactaldehyde as substrate. Shows expanded substrate
FT specificity."
FT /evidence="ECO:0000269|PubMed:27671251"
FT MUTAGEN 286
FT /note="N->H: 15-fold increase in catalytic efficiency with
FT L-lactaldehyde as substrate. Shows expanded substrate
FT specificity."
FT /evidence="ECO:0000269|PubMed:27671251"
FT MUTAGEN 286
FT /note="N->T: 6-fold increase in catalytic efficiency with
FT L-lactaldehyde as substrate. Shows expanded substrate
FT specificity."
FT /evidence="ECO:0000269|PubMed:27671251"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:2IMP"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 43..62
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 98..116
FT /evidence="ECO:0007829|PDB:2IMP"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 155..168
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2IMP"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 231..242
FT /evidence="ECO:0007829|PDB:2IMP"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 266..274
FT /evidence="ECO:0007829|PDB:2IMP"
FT TURN 279..282
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 298..310
FT /evidence="ECO:0007829|PDB:2IMP"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 331..346
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 386..396
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 397..405
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 407..416
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 432..439
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 456..458
FT /evidence="ECO:0007829|PDB:2IMP"
FT HELIX 462..467
FT /evidence="ECO:0007829|PDB:2IMP"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:2IMP"
SQ SEQUENCE 479 AA; 52273 MW; DA7819EA0C05C32F CRC64;
MSVPVQHPMY IDGQFVTWRG DAWIDVVNPA TEAVISRIPD GQAEDARKAI DAAERAQPEW
EALPAIERAS WLRKISAGIR ERASEISALI VEEGGKIQQL AEVEVAFTAD YIDYMAEWAR
RYEGEIIQSD RPGENILLFK RALGVTTGIL PWNFPFFLIA RKMAPALLTG NTIVIKPSEF
TPNNAIAFAK IVDEIGLPRG VFNLVLGRGE TVGQELAGNP KVAMVSMTGS VSAGEKIMAT
AAKNITKVCL ELGGKAPAIV MDDADLELAV KAIVDSRVIN SGQVCNCAER VYVQKGIYDQ
FVNRLGEAMQ AVQFGNPAER NDIAMGPLIN AAALERVEQK VARAVEEGAR VAFGGKAVEG
KGYYYPPTLL LDVRQEMSIM HEETFGPVLP VVAFDTLEDA ISMANDSDYG LTSSIYTQNL
NVAMKAIKGL KFGETYINRE NFEAMQGFHA GWRKSGIGGA DGKHGLHEYL QTQVVYLQS
