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 10-MAY-2017, entry version 148.
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};
GN 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;
RA Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
RT "Nucleotide sequence and transcriptional organization of the
RT Escherichia 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,
RP AND SUBUNIT.
RX PubMed=2521622;
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
RT product 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.,
RA Mau B., 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
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
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.,
RA Berchtold G.A., 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
RT protein-protein interaction between Escherichia coli 2,3-dihydro-2,3-
RT dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP
RT ligase (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
CC enterobactin (enterochelin), which is a macrocyclic trimeric
CC lactone of N-(2,3-dihydroxybenzoyl)-serine. Catalyzes the
CC reversible NAD-dependent oxidation of the C3-hydroxyl group of
CC 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), producing the
CC transient intermediate 2-hydroxy-3-oxo-4,6-cyclohexadiene-1-
CC carboxylate, which undergoes rapid aromatization to the final
CC product, 2,3-dihydroxybenzoate (2,3-DHB). Only the compounds with
CC a C3-hydroxyl group such as methyl 2,3-dihydro-2,3-
CC dihydroxybenzoate, methyl-3-hydroxy-1,4-cyclohexadiene-1-
CC carboxylate, trans-3-hydroxy-2-cyclohexene-1-carboxylate, cis-3-
CC hydroxy-4-cyclohexene-1-carboxylate, cis-3-hydroxycyclohexane-1-
CC carboxylic acid are oxidized to the corresponding ketone products.
CC The stereospecificity of the C3 allylic alcohol group oxidation is
CC 3R in a 1R,3R dihydro substrate. It can also increase the DHB-AMP
CC ligase activity of EntE by interaction EntE.
CC {ECO:0000269|PubMed:21166461, ECO:0000269|PubMed:2144454,
CC ECO:0000269|PubMed:2521622}.
CC -!- CATALYTIC ACTIVITY: 2,3-dihydro-2,3-dihydroxybenzoate + NAD(+) =
CC 2,3-dihydroxybenzoate + NADH. {ECO:0000269|PubMed:2144454}.
CC -!- ENZYME 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
CC 7.4 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
CC 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=1.7 mM for methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate
CC (at 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
CC 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=2.8 mM for cis-3-hydroxy-4-cyclohexene-1-carboxylate (at pH
CC 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=4.1 mM for cis-3-hydroxycyclohexane-1-carboxylic acid (at pH
CC 7.4 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
CC 37 degrees Celsius) {ECO:0000269|PubMed:2144454};
CC KM=25.2 mM for trans-3-hydroxycyclohexane-1-carboxylic acid (at
CC pH 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
CC Celsius) {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
CC degrees Celsius). Kcat is 1380 min(-1) for dehydrogenase
CC activity with cis-3-hydroxy-4-cyclohexene-1-carboxylate as
CC substrate (at pH 7.4 and 37 degrees Celsius). Kcat is 1050 min(-
CC 1) for dehydrogenase activity with 2,3-dihydro-2,3-
CC dihydroxybenzoate as substrate (at pH 7.4 and 37 degrees
CC Celsius). Kcat is 1000 min(-1) for dehydrogenase activity with
CC 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
CC with trans-3-hydroxy-2-cyclohexene-1-carboxylate and cis-3-
CC hydroxycyclohexane-1-carboxylic acid as substrates (at pH 7.4
CC and 37 degrees Celsius). Kcat is 180 min(-1) for dehydrogenase
CC activity with methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate
CC as substrate (at pH 7.4 and 37 degrees Celsius). Kcat is 60
CC min(-1) for dehydrogenase activity with trans-3,5-
CC cyclohexadiene-1,2-diol and 2-cyclohexen-1-ol as substrates (at
CC pH 7.4 and 37 degrees Celsius). Kcat is 44 min(-1) for
CC 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,
CC ECO:0000269|PubMed:21166461, ECO:0000269|PubMed:2521622}.
CC -!- INDUCTION: Under conditions of iron deficiency and by the fur
CC protein. {ECO:0000269|PubMed:2521621}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC (SDR) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40796.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; 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_LN832404.1.
DR PDB; 2FWM; X-ray; 2.00 A; X=1-248.
DR PDBsum; 2FWM; -.
DR ProteinModelPortal; P15047; -.
DR SMR; P15047; -.
DR BioGrid; 4260984; 134.
DR DIP; DIP-9511N; -.
DR IntAct; P15047; 8.
DR STRING; 511145.b0596; -.
DR EPD; 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; 32116368; VBIEscCol129921_0624.
DR EchoBASE; EB0255; -.
DR EcoGene; EG10259; entA.
DR eggNOG; ENOG4105X17; Bacteria.
DR eggNOG; COG1028; LUCA.
DR InParanoid; P15047; -.
DR KO; K00216; -.
DR OMA; ACAREMV; -.
DR PhylomeDB; P15047; -.
DR BioCyc; EcoCyc:ENTA-MONOMER; -.
DR BioCyc; MetaCyc:ENTA-MONOMER; -.
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: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; IMP:EcoCyc.
DR InterPro; IPR003560; DHB_DH.
DR InterPro; IPR016040; NAD(P)-bd_dom.
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; Complete proteome; Direct protein sequencing;
KW Enterobactin biosynthesis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1 248 2,3-dihydro-2,3-dihydroxybenzoate
FT dehydrogenase.
FT /FTId=PRO_0000054659.
FT NP_BIND 9 33 NAD. {ECO:0000250}.
FT ACT_SITE 144 144 Proton acceptor. {ECO:0000255|PROSITE-
FT ProRule:PRU10001}.
FT BINDING 131 131 Substrate. {ECO:0000250}.
FT STRAND 7 12 {ECO:0000244|PDB:2FWM}.
FT HELIX 16 27 {ECO:0000244|PDB:2FWM}.
FT STRAND 31 37 {ECO:0000244|PDB:2FWM}.
FT STRAND 45 50 {ECO:0000244|PDB:2FWM}.
FT HELIX 56 69 {ECO:0000244|PDB:2FWM}.
FT STRAND 75 78 {ECO:0000244|PDB:2FWM}.
FT TURN 88 90 {ECO:0000244|PDB:2FWM}.
FT HELIX 93 103 {ECO:0000244|PDB:2FWM}.
FT HELIX 105 121 {ECO:0000244|PDB:2FWM}.
FT STRAND 125 129 {ECO:0000244|PDB:2FWM}.
FT HELIX 132 134 {ECO:0000244|PDB:2FWM}.
FT HELIX 142 162 {ECO:0000244|PDB:2FWM}.
FT HELIX 163 165 {ECO:0000244|PDB:2FWM}.
FT STRAND 168 174 {ECO:0000244|PDB:2FWM}.
FT HELIX 215 226 {ECO:0000244|PDB:2FWM}.
FT HELIX 228 230 {ECO:0000244|PDB:2FWM}.
FT STRAND 237 241 {ECO:0000244|PDB:2FWM}.
FT TURN 242 247 {ECO:0000244|PDB:2FWM}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 131 159 ipat:ADH_SHORT [T]
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
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