ENTA_ECOLI
ID ENTA_ECOLI Reviewed; 248 AA.
AC P15047; P77100; Q2MBK5;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase {ECO:0000303|PubMed:2521622};
DE Short=DiDHB-DH {ECO:0000303|PubMed:2521622};
DE EC=1.3.1.28 {ECO:0000269|PubMed:2144454};
DE AltName: Full=Trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase {ECO:0000303|PubMed:2144454};
GN Name=entA {ECO:0000303|PubMed:2521622}; OrderedLocusNames=b0596, JW0588;
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 INDUCTION.
RX PubMed=2521621; DOI=10.1128/jb.171.2.784-790.1989;
RA Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT "Nucleotide sequence and transcriptional organization of the Escherichia
RT coli enterobactin biosynthesis cistrons entB and entA.";
RL J. Bacteriol. 171:784-790(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14, FUNCTION, AND
RP SUBUNIT.
RX PubMed=2521622; DOI=10.1128/jb.171.2.791-798.1989;
RA Liu J., Duncan K., Walsh C.T.;
RT "Nucleotide sequence of a cluster of Escherichia coli enterobactin
RT biosynthesis genes: identification of entA and purification of its product
RT 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.";
RL J. Bacteriol. 171:791-798(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBSTRATE SPECIFICITY.
RX PubMed=2144454; DOI=10.1021/bi00481a006;
RA Sakaitani M., Rusnak F., Quinn N.R., Tu C., Frigo T.B., Berchtold G.A.,
RA Walsh C.T.;
RT "Mechanistic studies on trans-2,3-dihydro-2,3-dihydroxybenzoate
RT dehydrogenase (EntA) in the biosynthesis of the iron chelator
RT enterobactin.";
RL Biochemistry 29:6789-6798(1990).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=21166461; DOI=10.1021/bi101558v;
RA Khalil S., Pawelek P.D.;
RT "Enzymatic adenylation of 2,3-dihydroxybenzoate is enhanced by a protein-
RT protein interaction between Escherichia coli 2,3-dihydro-2,3-
RT dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP ligase
RT (EntE).";
RL Biochemistry 50:533-545(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND SUBUNIT.
RX PubMed=16790929; DOI=10.1107/s0907444906015824;
RA Sundlov J.A., Garringer J.A., Carney J.M., Reger A.S., Drake E.J.,
RA Duax W.L., Gulick A.M.;
RT "Determination of the crystal structure of EntA, a 2,3-dihydro-2,3-
RT dihydroxybenzoic acid dehydrogenase from Escherichia coli.";
RL Acta Crystallogr. D 62:734-740(2006).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore enterobactin
CC (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-
CC dihydroxybenzoyl)-serine. Catalyzes the reversible NAD-dependent
CC oxidation of the C3-hydroxyl group of 2,3-dihydro-2,3-dihydroxybenzoate
CC (2,3-diDHB), producing the transient intermediate 2-hydroxy-3-oxo-4,6-
CC cyclohexadiene-1-carboxylate, which undergoes rapid aromatization to
CC the final product, 2,3-dihydroxybenzoate (2,3-DHB). Only the compounds
CC with a C3-hydroxyl group such as methyl 2,3-dihydro-2,3-
CC dihydroxybenzoate, methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate,
CC trans-3-hydroxy-2-cyclohexene-1-carboxylate, cis-3-hydroxy-4-
CC cyclohexene-1-carboxylate, cis-3-hydroxycyclohexane-1-carboxylic acid
CC are oxidized to the corresponding ketone products. The
CC stereospecificity of the C3 allylic alcohol group oxidation is 3R in a
CC 1R,3R dihydro substrate. It can also increase the DHB-AMP ligase
CC activity of EntE by interaction EntE. {ECO:0000269|PubMed:21166461,
CC ECO:0000269|PubMed:2144454, ECO:0000269|PubMed:2521622}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD(+) = 2,3-
CC dihydroxybenzoate + H(+) + NADH; Xref=Rhea:RHEA:23824,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36654, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58764; EC=1.3.1.28;
CC Evidence={ECO:0000269|PubMed:2144454};
CC -!- ACTIVITY REGULATION: Inhibited by cis-2-hydroxy-3-cyclohexen-1-
CC carboxylate, cis-2-hydroxycyclohexane-1-carboxylate and trans-2-
CC hydroxycyclohexane-1-carboxylate. {ECO:0000269|PubMed:2144454}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for methyl 2,3-dihydro-2,3-dihydroxybenzoate (at pH 7.4
CC and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=0.3 mM for 2,3-dihydro-2,3-dihydroxybenzoate (at pH 7.4 and 37
CC degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=1.7 mM for methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate (at
CC pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=1.9 mM for trans-3-hydroxy-2-cyclohexene-1-carboxylate (at pH 7.4
CC and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=2.8 mM for cis-3-hydroxy-4-cyclohexene-1-carboxylate (at pH 7.4
CC and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=4.1 mM for cis-3-hydroxycyclohexane-1-carboxylic acid (at pH 7.4
CC and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=16.5 mM for trans-3,5-cyclohexadiene-1,2-diol (at pH 7.4 and 37
CC degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=25.2 mM for trans-3-hydroxycyclohexane-1-carboxylic acid (at pH
CC 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=83.3 mM for 2-cyclohexen-1-ol (at pH 7.4 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2144454};
CC KM=168 mM for cis-3,5-cyclohexadiene-1,2-diol (at pH 7.4 and 37
CC degrees Celsius) {ECO:0000269|PubMed:2144454};
CC Note=kcat is 5550 min(-1) for dehydrogenase activity with 2,3-
CC dihydro-2,3-dihydroxybenzoate as substrate (at pH 7.4 and 37 degrees
CC Celsius). kcat is 1380 min(-1) for dehydrogenase activity with cis-3-
CC hydroxy-4-cyclohexene-1-carboxylate as substrate (at pH 7.4 and 37
CC degrees Celsius). kcat is 1050 min(-1) for dehydrogenase activity
CC with 2,3-dihydro-2,3-dihydroxybenzoate as substrate (at pH 7.4 and 37
CC degrees Celsius). kcat is 1000 min(-1) for dehydrogenase activity
CC with cis-3,5-cyclohexadiene-1,2-diol as substrate (at pH 7.4 and 37
CC degrees Celsius). kcat is 300 min(-1) for dehydrogenase activity with
CC trans-3-hydroxy-2-cyclohexene-1-carboxylate and cis-3-
CC hydroxycyclohexane-1-carboxylic acid as substrates (at pH 7.4 and 37
CC degrees Celsius). kcat is 180 min(-1) for dehydrogenase activity with
CC methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate as substrate (at pH
CC 7.4 and 37 degrees Celsius). kcat is 60 min(-1) for dehydrogenase
CC activity with trans-3,5-cyclohexadiene-1,2-diol and 2-cyclohexen-1-ol
CC as substrates (at pH 7.4 and 37 degrees Celsius). kcat is 44 min(-1)
CC for dehydrogenase activity with trans-3-hydroxycyclohexane-1-
CC carboxylic acid as substrate (at pH 7.4 and 37 degrees Celsius).
CC {ECO:0000269|PubMed:2144454};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. EntA and EntE interact
CC together. {ECO:0000269|PubMed:16790929, ECO:0000269|PubMed:21166461,
CC ECO:0000269|PubMed:2521622}.
CC -!- INTERACTION:
CC P15047; P15047: entA; NbExp=4; IntAct=EBI-1118936, EBI-1118936;
CC P15047; P10378: entE; NbExp=5; IntAct=EBI-1118936, EBI-550322;
CC -!- INDUCTION: Under conditions of iron deficiency and by the fur protein.
CC {ECO:0000269|PubMed:2521621}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M24148; AAA16103.1; -; Unassigned_DNA.
DR EMBL; M24143; AAA76836.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40796.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73697.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76351.1; -; Genomic_DNA.
DR PIR; A91904; DEECDB.
DR RefSeq; NP_415128.1; NC_000913.3.
DR RefSeq; WP_000347651.1; NZ_SSZK01000032.1.
DR PDB; 2FWM; X-ray; 2.00 A; X=1-248.
DR PDBsum; 2FWM; -.
DR AlphaFoldDB; P15047; -.
DR SMR; P15047; -.
DR BioGRID; 4260984; 137.
DR BioGRID; 849662; 3.
DR ComplexPortal; CPX-5747; entAE 2,3-dihydroxybenzoate-AMP ligase complex.
DR DIP; DIP-9511N; -.
DR IntAct; P15047; 10.
DR STRING; 511145.b0596; -.
DR jPOST; P15047; -.
DR PaxDb; P15047; -.
DR PRIDE; P15047; -.
DR EnsemblBacteria; AAC73697; AAC73697; b0596.
DR EnsemblBacteria; BAE76351; BAE76351; BAE76351.
DR GeneID; 945284; -.
DR KEGG; ecj:JW0588; -.
DR KEGG; eco:b0596; -.
DR PATRIC; fig|1411691.4.peg.1673; -.
DR EchoBASE; EB0255; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_0_6; -.
DR InParanoid; P15047; -.
DR OMA; ICPGIIE; -.
DR PhylomeDB; P15047; -.
DR BioCyc; EcoCyc:ENTA-MON; -.
DR BioCyc; MetaCyc:ENTA-MON; -.
DR UniPathway; UPA00017; -.
DR EvolutionaryTrace; P15047; -.
DR PRO; PR:P15047; -.
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:0008667; F:2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0009239; P:enterobactin biosynthetic process; IDA:ComplexPortal.
DR CDD; cd05331; DH-DHB-DH_SDR_c; 1.
DR InterPro; IPR003560; DHB_DH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR01397; DHBDHDRGNASE.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR04316; dhbA_paeA; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Enterobactin biosynthesis; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..248
FT /note="2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase"
FT /id="PRO_0000054659"
FT ACT_SITE 144
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 9..33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:2FWM"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2FWM"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 56..69
FT /evidence="ECO:0007829|PDB:2FWM"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2FWM"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 105..121
FT /evidence="ECO:0007829|PDB:2FWM"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 142..162
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2FWM"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:2FWM"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:2FWM"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:2FWM"
FT TURN 242..247
FT /evidence="ECO:0007829|PDB:2FWM"
SQ SEQUENCE 248 AA; 26250 MW; E840488335AD317B CRC64;
MDFSGKNVWV TGAGKGIGYA TALAFVEAGA KVTGFDQAFT QEQYPFATEV MDVADAAQVA
QVCQRLLAET ERLDALVNAA GILRMGATDQ LSKEDWQQTF AVNVGGAFNL FQQTMNQFRR
QRGGAIVTVA SDAAHTPRIG MSAYGASKAA LKSLALSVGL ELAGSGVRCN VVSPGSTDTD
MQRTLWVSDD AEEQRIRGFG EQFKLGIPLG KIARPQEIAN TILFLASDLA SHITLQDIVV
DGGSTLGA
