LGOD_ECOLI
ID LGOD_ECOLI Reviewed; 340 AA.
AC P39400; Q2M5V8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=L-galactonate-5-dehydrogenase {ECO:0000303|PubMed:24861318};
DE EC=1.1.1.414 {ECO:0000269|PubMed:24861318};
GN Name=lgoD; Synonyms=yjjN; OrderedLocusNames=b4358, JW5793;
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;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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, ROLE IN L-GALACTONATE UTILIZATION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RX PubMed=17088549; DOI=10.1073/pnas.0603364103;
RA Reed J.L., Patel T.R., Chen K.H., Joyce A.R., Applebee M.K., Herring C.D.,
RA Bui O.T., Knight E.M., Fong S.S., Palsson B.O.;
RT "Systems approach to refining genome annotation.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17480-17484(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=24861318; DOI=10.1007/s12010-014-0969-0;
RA Kuivanen J., Richard P.;
RT "The yjjN of E. coli codes for an L-galactonate dehydrogenase and can be
RT used for quantification of L-galactonate and L-gulonate.";
RL Appl. Biochem. Biotechnol. 173:1829-1835(2014).
CC -!- FUNCTION: Catalyzes the oxidation of L-galactonate to D-tagaturonate.
CC Required for growth on L-galactonate as the sole carbon source. In
CC vitro, can also use L-gulonate. {ECO:0000269|PubMed:17088549,
CC ECO:0000269|PubMed:24861318}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-galactonate + NAD(+) = H(+) + keto-D-tagaturonate + NADH;
CC Xref=Rhea:RHEA:30183, ChEBI:CHEBI:15378, ChEBI:CHEBI:17886,
CC ChEBI:CHEBI:53071, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.1.1.414; Evidence={ECO:0000269|PubMed:24861318};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:24861318}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.5 mM for L-galactonate {ECO:0000269|PubMed:24861318};
CC Vmax=0.8 umol/min/mg enzyme {ECO:0000269|PubMed:24861318};
CC Note=kcat is 0.51 sec(-1) with L-galactonate.
CC {ECO:0000269|PubMed:24861318};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:24861318};
CC -!- INDUCTION: Highly up-regulated during growth on L-galactonate.
CC {ECO:0000269|PubMed:17088549}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on L-
CC galactonate as sole carbon source. {ECO:0000269|PubMed:17088549}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97256.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97256.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77314.4; -; Genomic_DNA.
DR EMBL; AP009048; BAE78348.1; -; Genomic_DNA.
DR PIR; S56585; S56585.
DR RefSeq; NP_418778.4; NC_000913.3.
DR RefSeq; WP_000106030.1; NZ_STEB01000025.1.
DR AlphaFoldDB; P39400; -.
DR SMR; P39400; -.
DR BioGRID; 4261389; 22.
DR STRING; 511145.b4358; -.
DR PaxDb; P39400; -.
DR PRIDE; P39400; -.
DR EnsemblBacteria; AAC77314; AAC77314; b4358.
DR EnsemblBacteria; BAE78348; BAE78348; BAE78348.
DR GeneID; 948883; -.
DR KEGG; ecj:JW5793; -.
DR KEGG; eco:b4358; -.
DR PATRIC; fig|1411691.4.peg.2328; -.
DR EchoBASE; EB2475; -.
DR eggNOG; COG1063; Bacteria.
DR HOGENOM; CLU_026673_11_0_6; -.
DR InParanoid; P39400; -.
DR OMA; THCENRT; -.
DR PhylomeDB; P39400; -.
DR BioCyc; EcoCyc:G7945-MON; -.
DR BioCyc; MetaCyc:G7945-MON; -.
DR PRO; PR:P39400; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034195; P:L-galactonate catabolic process; IMP:EcoCyc.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..340
FT /note="L-galactonate-5-dehydrogenase"
FT /id="PRO_0000160895"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 36448 MW; 15FD289EFFD05567 CRC64;
MSTMNVLICQ QPKELVWKQR EIPIPGDNEA LIKIKSVGIC GTDIHAWGGN QPFFSYPRVL
GHEICGEIVG LGKNIADLKN GQQVAVIPYV ACQQCPACKS GRTNCCEKIS VIGVHQDGGF
SEYLSVPVAN ILPADGIDPQ AAALIEPFAI SAHAVRRAAI APGEQVLVVG AGPIGLGAAA
IAKADGAQVV VADTSPARRE HVATRLELPL LDPSAEDFDA QLRAQFGGSL AQKVIDATGN
QHAMNNTVNL IRHGGTVVFV GLFKGELQFS DPEFHKKETT MMGSRNATPE DFAKVGRLMA
EGKITADMML THRYPFATLA ETYERDVINN RELIKGVITF
