FUCO_ECOLI
ID FUCO_ECOLI Reviewed; 382 AA.
AC P0A9S1; P11549; Q2MA35;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Lactaldehyde reductase;
DE EC=1.1.1.77;
DE AltName: Full=Propanediol oxidoreductase;
GN Name=fucO; OrderedLocusNames=b2799, JW2770;
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=2553671; DOI=10.1128/jb.171.11.6097-6105.1989;
RA Chen Y.M., Lu Z., Lin E.C.C.;
RT "Constitutive activation of the fucAO operon and silencing of the
RT divergently transcribed fucPIK operon by an IS5 element in Escherichia coli
RT mutants selected for growth on L-1,2-propanediol.";
RL J. Bacteriol. 171:6097-6105(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2664711; DOI=10.1093/nar/17.12.4883;
RA Lu Z., Lin E.C.C.;
RT "The nucleotide sequence of Escherichia coli genes for L-fucose
RT dissimilation.";
RL Nucleic Acids Res. 17:4883-4884(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2661535; DOI=10.1128/jb.171.7.3754-3759.1989;
RA Conway T., Ingram L.O.;
RT "Similarity of Escherichia coli propanediol oxidoreductase (fucO product)
RT and an unusual alcohol dehydrogenase from Zymomonas mobilis and
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 171:3754-3759(1989).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-382.
RC STRAIN=K12;
RX PubMed=8385012; DOI=10.1111/j.1432-1033.1993.tb17718.x;
RA Shao Z., Newman E.B.;
RT "Sequencing and characterization of the sdaB gene from Escherichia coli K-
RT 12.";
RL Eur. J. Biochem. 212:777-784(1993).
RN [7] {ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4}
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH NAD(+), COFACTOR,
RP SUBUNIT, ACTIVITY REGULATION, AND MUTAGENESIS OF 1-MET--ASN-9; GLY-16;
RP ASP-38; GLY-96; ASP-195 AND HIS-199.
RC STRAIN=K12 / ECL1;
RX PubMed=15995211; DOI=10.1128/jb.187.14.4957-4966.2005;
RA Montella C., Bellsolell L., Perez-Luque R., Badia J., Baldoma L., Coll M.,
RA Aguilar J.;
RT "Crystal structure of an iron-dependent group III dehydrogenase that
RT interconverts L-lactaldehyde and L-1,2-propanediol in Escherichia coli.";
RL J. Bacteriol. 187:4957-4966(2005).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of lactaldehyde reductase.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-propane-1,2-diol + NAD(+) = (R)-lactaldehyde + H(+) +
CC NADH; Xref=Rhea:RHEA:23872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17167,
CC ChEBI:CHEBI:28972, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.77;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-propane-1,2-diol + NAD(+) = (S)-lactaldehyde + H(+) +
CC NADH; Xref=Rhea:RHEA:15933, ChEBI:CHEBI:15378, ChEBI:CHEBI:18041,
CC ChEBI:CHEBI:29002, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.77;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:15995211};
CC -!- ACTIVITY REGULATION: Inhibited by Zn(2+).
CC {ECO:0000269|PubMed:15995211}.
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15995211}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23824.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA23825.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB40449.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE76871.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA33124.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M31059; AAA23824.1; ALT_INIT; Genomic_DNA.
DR EMBL; X15025; CAA33124.1; ALT_INIT; Genomic_DNA.
DR EMBL; M27177; AAA23825.1; ALT_INIT; Genomic_DNA.
DR EMBL; U29581; AAB40449.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75841.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76871.1; ALT_INIT; Genomic_DNA.
DR EMBL; L07763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A32883; RDECLA.
DR RefSeq; NP_417279.2; NC_000913.3.
DR RefSeq; WP_000013588.1; NZ_STEB01000030.1.
DR PDB; 1RRM; X-ray; 1.60 A; A/B=1-382.
DR PDB; 2BI4; X-ray; 2.85 A; A/B=1-382.
DR PDB; 2BL4; X-ray; 2.85 A; A/B=1-382.
DR PDB; 5BR4; X-ray; 0.91 A; A/B=1-382.
DR PDBsum; 1RRM; -.
DR PDBsum; 2BI4; -.
DR PDBsum; 2BL4; -.
DR PDBsum; 5BR4; -.
DR AlphaFoldDB; P0A9S1; -.
DR SMR; P0A9S1; -.
DR BioGRID; 4259223; 91.
DR BioGRID; 851603; 2.
DR DIP; DIP-48076N; -.
DR IntAct; P0A9S1; 5.
DR STRING; 511145.b2799; -.
DR DrugBank; DB02059; Adenosine-5-Diphosphoribose.
DR jPOST; P0A9S1; -.
DR PaxDb; P0A9S1; -.
DR PRIDE; P0A9S1; -.
DR EnsemblBacteria; AAC75841; AAC75841; b2799.
DR EnsemblBacteria; BAE76871; BAE76871; BAE76871.
DR GeneID; 66673334; -.
DR GeneID; 947273; -.
DR KEGG; ecj:JW2770; -.
DR KEGG; eco:b2799; -.
DR PATRIC; fig|1411691.4.peg.3934; -.
DR EchoBASE; EB0347; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_6; -.
DR InParanoid; P0A9S1; -.
DR OMA; PGELMDY; -.
DR PhylomeDB; P0A9S1; -.
DR BioCyc; EcoCyc:LACTALDREDUCT-MON; -.
DR BioCyc; MetaCyc:LACTALDREDUCT-MON; -.
DR UniPathway; UPA00563; -.
DR EvolutionaryTrace; P0A9S1; -.
DR PRO; PR:P0A9S1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0008912; F:lactaldehyde reductase activity; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0052660; F:R-lactaldehyde reductase activity; IEA:RHEA.
DR GO; GO:0052661; F:S-lactaldehyde reductase activity; IEA:RHEA.
DR GO; GO:0042846; P:glycol catabolic process; IDA:EcoCyc.
DR GO; GO:0042355; P:L-fucose catabolic process; IMP:EcoCyc.
DR GO; GO:0051143; P:propanediol metabolic process; IDA:EcoCyc.
DR GO; GO:0019301; P:rhamnose catabolic process; IEP:EcoCyc.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR013460; Lactal_redase.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR TIGRFAMs; TIGR02638; lactal_redase; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Fucose metabolism; Iron;
KW Metal-binding; NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..382
FT /note="Lactaldehyde reductase"
FT /id="PRO_0000087824"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4,
FT ECO:0007744|PDB:5BR4"
FT BINDING 70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4"
FT BINDING 97..101
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4,
FT ECO:0007744|PDB:5BR4"
FT BINDING 139..143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4,
FT ECO:0007744|PDB:5BR4"
FT BINDING 148..150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4,
FT ECO:0007744|PDB:5BR4"
FT BINDING 180..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4,
FT ECO:0007744|PDB:5BR4"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:1RRM, ECO:0007744|PDB:2BI4,
FT ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:1RRM, ECO:0007744|PDB:2BI4,
FT ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:1RRM, ECO:0007744|PDB:2BI4,
FT ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4"
FT BINDING 276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0007744|PDB:1RRM, ECO:0007744|PDB:2BI4,
FT ECO:0007744|PDB:2BL4, ECO:0007744|PDB:5BR4"
FT BINDING 276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4,
FT ECO:0007744|PDB:5BR4"
FT BINDING 341
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:2BI4, ECO:0007744|PDB:2BL4"
FT MUTAGEN 1..9
FT /note="MANRMILNE->M: Loss of enzyme activity, loss of
FT dimerization."
FT /evidence="ECO:0000269|PubMed:15995211"
FT MUTAGEN 16
FT /note="G->D: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:15995211"
FT MUTAGEN 38
FT /note="D->G: Enzyme can now use NADP."
FT /evidence="ECO:0000269|PubMed:15995211"
FT MUTAGEN 96
FT /note="G->E: Loss of NAD binding and enzyme activity."
FT /evidence="ECO:0000269|PubMed:15995211"
FT MUTAGEN 195
FT /note="D->L: Complete loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:15995211"
FT MUTAGEN 199
FT /note="H->A,F: Complete loss of iron-binding."
FT /evidence="ECO:0000269|PubMed:15995211"
FT CONFLICT 273
FT /note="N -> T (in Ref. 2; CAA33124)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1RRM"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1RRM"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1RRM"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:5BR4"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:5BR4"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 186..205
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 211..232
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 236..256
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 276..291
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 298..305
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 315..333
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 349..358
FT /evidence="ECO:0007829|PDB:5BR4"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:5BR4"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2BL4"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:5BR4"
SQ SEQUENCE 382 AA; 40513 MW; E4D927AC8142098B CRC64;
MANRMILNET AWFGRGAVGA LTDEVKRRGY QKALIVTDKT LVQCGVVAKV TDKMDAAGLA
WAIYDGVVPN PTITVVKEGL GVFQNSGADY LIAIGGGSPQ DTCKAIGIIS NNPEFADVRS
LEGLSPTNKP SVPILAIPTT AGTAAEVTIN YVITDEEKRR KFVCVDPHDI PQVAFIDADM
MDGMPPALKA ATGVDALTHA IEGYITRGAW ALTDALHIKA IEIIAGALRG SVAGDKDAGE
EMALGQYVAG MGFSNVGLGL VHGMAHPLGA FYNTPHGVAN AILLPHVMRY NADFTGEKYR
DIARVMGVKV EGMSLEEARN AAVEAVFALN RDVGIPPHLR DVGVRKEDIP ALAQAALDDV
CTGGNPREAT LEDIVELYHT AW
