FUCO_ECO57
ID FUCO_ECO57 Reviewed; 382 AA.
AC P0A9S2; P11549;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Lactaldehyde reductase;
DE EC=1.1.1.77;
DE AltName: Full=Propanediol oxidoreductase;
GN Name=fucO; OrderedLocusNames=Z4116, ECs3659;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG57913.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB37082.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57913.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37082.1; ALT_INIT; Genomic_DNA.
DR PIR; C91086; C91086.
DR PIR; E85931; E85931.
DR RefSeq; NP_311686.2; NC_002695.1.
DR RefSeq; WP_000013588.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0A9S2; -.
DR SMR; P0A9S2; -.
DR STRING; 155864.EDL933_3980; -.
DR DNASU; 958299; -.
DR EnsemblBacteria; AAG57913; AAG57913; Z4116.
DR EnsemblBacteria; BAB37082; BAB37082; ECs_3659.
DR GeneID; 66673334; -.
DR GeneID; 916534; -.
DR KEGG; ece:Z4116; -.
DR KEGG; ecs:ECs_3659; -.
DR PATRIC; fig|386585.9.peg.3825; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_6; -.
DR OMA; PGELMDY; -.
DR UniPathway; UPA00563; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0046872; F:metal ion 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:0019317; P:fucose catabolic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Fucose metabolism; Iron; Metal-binding; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..382
FT /note="Lactaldehyde reductase"
FT /id="PRO_0000087825"
FT BINDING 38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 97..98
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 139..143
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 180..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
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
