ENTH_ECOLI
ID ENTH_ECOLI Reviewed; 137 AA.
AC P0A8Y8; P15050; Q2MBK4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Proofreading thioesterase EntH {ECO:0000255|HAMAP-Rule:MF_00907};
DE EC=3.1.2.- {ECO:0000255|HAMAP-Rule:MF_00907};
DE AltName: Full=Enterobactin synthase component H {ECO:0000255|HAMAP-Rule:MF_00907};
DE AltName: Full=p15;
GN Name=entH {ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000303|PubMed:17675380};
GN Synonyms=ybdB; OrderedLocusNames=b0597, JW0589;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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].
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 AS AN ESTERASE.
RX PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT "Enzyme genomics: application of general enzymatic screens to discover new
RT enzymes.";
RL FEMS Microbiol. Rev. 29:263-279(2005).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, INTERACTION WITH ENTB,
RP SUBCELLULAR LOCATION, INDUCTION, AND GENE NAME.
RC STRAIN=K12;
RX PubMed=17675380; DOI=10.1128/jb.00755-07;
RA Leduc D., Battesti A., Bouveret E.;
RT "The hotdog thioesterase EntH (YbdB) plays a role in vivo in optimal
RT enterobactin biosynthesis by interacting with the ArCP domain of EntB.";
RL J. Bacteriol. 189:7112-7126(2007).
RN [8]
RP FUNCTION AS AN ESTERASE, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19119850; DOI=10.1021/bi802207t;
RA Chen D., Wu R., Bryan T.L., Dunaway-Mariano D.;
RT "In vitro kinetic analysis of substrate specificity in enterobactin
RT biosynthetic lower pathway enzymes provides insight into the biochemical
RT function of the hot dog-fold thioesterase EntH.";
RL Biochemistry 48:511-513(2009).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF GLN-48; HIS-54; GLU-63; THR-64; SER-67 AND MET-68.
RC STRAIN=K12;
RX PubMed=19193103; DOI=10.1021/bi802165x;
RA Guo Z.F., Sun Y., Zheng S., Guo Z.;
RT "Preferential hydrolysis of aberrant intermediates by the type II
RT thioesterase in Escherichia coli nonribosomal enterobactin synthesis:
RT substrate specificities and mutagenic studies on the active-site
RT residues.";
RL Biochemistry 48:1712-1722(2009).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF MET-68.
RX PubMed=24992697; DOI=10.1021/bi500333m;
RA Latham J.A., Chen D., Allen K.N., Dunaway-Mariano D.;
RT "Divergence of substrate specificity and function in the Escherichia coli
RT hotdog-fold thioesterase paralogs YdiI and YbdB.";
RL Biochemistry 53:4775-4787(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-137.
RA Murshudov G.N., Vagin A.A., Dodson E.J.;
RT "Crystal structure of a putative thioesterase.";
RL Submitted (DEC-2003) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH SUBSTRATE ANALOGS,
RP SUBUNIT, MUTAGENESIS OF GLN-48; HIS-54; GLU-63 AND MET-68, AND ACTIVE SITE.
RX PubMed=25010423; DOI=10.1021/bi500334v;
RA Wu R., Latham J.A., Chen D., Farelli J., Zhao H., Matthews K., Allen K.N.,
RA Dunaway-Mariano D.;
RT "Structure and catalysis in the Escherichia coli hotdog-fold thioesterase
RT paralogs YdiI and YbdB.";
RL Biochemistry 53:4788-4805(2014).
CC -!- FUNCTION: Required for optimal enterobactin synthesis. Acts as a
CC proofreading enzyme that prevents EntB misacylation by hydrolyzing the
CC thioester bound existing between EntB and wrongly charged molecules.
CC Displays esterase activity toward a wide range of substrates, including
CC acyl-CoAs and aryl-CoAs. {ECO:0000269|PubMed:15808744,
CC ECO:0000269|PubMed:17675380, ECO:0000269|PubMed:19119850,
CC ECO:0000269|PubMed:19193103, ECO:0000269|PubMed:24992697}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19119850};
CC KM=116 uM for 2,3-DHB-EntB {ECO:0000269|PubMed:19193103};
CC KM=21 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19119850};
CC KM=190 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=25 uM for 2,4-DHB-EntB {ECO:0000269|PubMed:19119850};
CC KM=32 uM for lauroyl-EntB {ECO:0000269|PubMed:19119850};
CC KM=35 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19119850};
CC KM=265 uM for 3-hydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=37 uM for 3-HPA-CoA {ECO:0000269|PubMed:19119850};
CC KM=45 uM for lauroyl-CoA {ECO:0000269|PubMed:19119850};
CC KM=49 uM for decanoyl-CoA {ECO:0000269|PubMed:19119850};
CC KM=55 uM for palmitoyl-CoA {ECO:0000269|PubMed:19119850};
CC KM=4.25 uM for palmitoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=161 uM for 2,3-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=176 uM for salicylyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=212 uM for 3,4-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=219 uM for 2,4-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=256 uM for 3,5-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=272 uM for salicylyl-EntB {ECO:0000269|PubMed:19193103};
CC KM=350 uM for hexanoyl-CoA {ECO:0000269|PubMed:19119850};
CC KM=400 uM for propionyl-CoA {ECO:0000269|PubMed:19119850};
CC KM=475 uM for benzoyl-CoA {ECO:0000269|PubMed:19193103};
CC KM=800 uM for acetyl-CoA {ECO:0000269|PubMed:19119850};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00907, ECO:0000269|PubMed:17675380}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. Interacts specifically with the
CC aryl carrier protein (ArCP) domain of EntB. {ECO:0000255|HAMAP-
CC Rule:MF_00907, ECO:0000269|PubMed:17675380,
CC ECO:0000269|PubMed:19193103, ECO:0000269|PubMed:25010423}.
CC -!- INTERACTION:
CC P0A8Y8; P0ADI4: entB; NbExp=3; IntAct=EBI-1118982, EBI-547993;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00907,
CC ECO:0000269|PubMed:17675380}.
CC -!- INDUCTION: Induced by iron starvation. {ECO:0000269|PubMed:17675380}.
CC -!- SIMILARITY: Belongs to the thioesterase PaaI family.
CC {ECO:0000255|HAMAP-Rule:MF_00907}.
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DR EMBL; M24148; AAA16104.1; -; Unassigned_DNA.
DR EMBL; M24143; AAA76837.1; -; Genomic_DNA.
DR EMBL; U82598; AAB40797.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73698.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76352.1; -; Genomic_DNA.
DR PIR; B91904; Q3ECEA.
DR RefSeq; NP_415129.1; NC_000913.3.
DR RefSeq; WP_000637953.1; NZ_STEB01000047.1.
DR PDB; 1VH9; X-ray; 2.15 A; A/B=2-137.
DR PDB; 4K4C; X-ray; 1.85 A; A/B/C/D=1-137.
DR PDB; 4K4D; X-ray; 2.17 A; A/B=1-137.
DR PDBsum; 1VH9; -.
DR PDBsum; 4K4C; -.
DR PDBsum; 4K4D; -.
DR AlphaFoldDB; P0A8Y8; -.
DR SMR; P0A8Y8; -.
DR BioGRID; 4260982; 15.
DR DIP; DIP-11343N; -.
DR IntAct; P0A8Y8; 2.
DR STRING; 511145.b0597; -.
DR PaxDb; P0A8Y8; -.
DR PRIDE; P0A8Y8; -.
DR EnsemblBacteria; AAC73698; AAC73698; b0597.
DR EnsemblBacteria; BAE76352; BAE76352; BAE76352.
DR GeneID; 67416358; -.
DR GeneID; 945215; -.
DR KEGG; ecj:JW0589; -.
DR KEGG; eco:b0597; -.
DR PATRIC; fig|1411691.4.peg.1672; -.
DR EchoBASE; EB1097; -.
DR eggNOG; COG2050; Bacteria.
DR HOGENOM; CLU_089876_13_1_6; -.
DR InParanoid; P0A8Y8; -.
DR OMA; QHGGVYC; -.
DR PhylomeDB; P0A8Y8; -.
DR BioCyc; EcoCyc:EG11105-MON; -.
DR BioCyc; MetaCyc:EG11105-MON; -.
DR BRENDA; 3.1.2.2; 2026.
DR BRENDA; 3.1.2.28; 2026.
DR SABIO-RK; P0A8Y8; -.
DR UniPathway; UPA00017; -.
DR EvolutionaryTrace; P0A8Y8; -.
DR PRO; PR:P0A8Y8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0061522; F:1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity; IBA:GO_Central.
DR GO; GO:0016289; F:CoA hydrolase activity; IDA:EcoCyc.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0016790; F:thiolester hydrolase activity; IDA:EcoCyc.
DR GO; GO:0009239; P:enterobactin biosynthetic process; IMP:EcoCyc.
DR HAMAP; MF_00907; Thioesterase_EntH; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR026576; Thioesterase_EntH.
DR InterPro; IPR006683; Thioestr_dom.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
DR TIGRFAMs; TIGR00369; unchar_dom_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..137
FT /note="Proofreading thioesterase EntH"
FT /id="PRO_0000156676"
FT ACT_SITE 63
FT /note="Nucleophile or proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00907,
FT ECO:0000303|PubMed:25010423, ECO:0000305|PubMed:19193103"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25010423"
FT BINDING 54..55
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25010423"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25010423"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25010423"
FT MUTAGEN 48
FT /note="Q->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19193103,
FT ECO:0000269|PubMed:25010423"
FT MUTAGEN 48
FT /note="Q->N: 290-fold decrease in activity toward
FT salicylyl-CoA."
FT /evidence="ECO:0000269|PubMed:19193103"
FT MUTAGEN 54
FT /note="H->A: 229-fold decrease in activity toward
FT salicylyl-CoA. Loss of activity toward benzoyl-CoA."
FT /evidence="ECO:0000269|PubMed:19193103,
FT ECO:0000269|PubMed:25010423"
FT MUTAGEN 63
FT /note="E->A,D,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:19193103,
FT ECO:0000269|PubMed:25010423"
FT MUTAGEN 64
FT /note="T->S: 13-fold decrease in activity toward salicylyl-
FT CoA."
FT /evidence="ECO:0000269|PubMed:19193103"
FT MUTAGEN 67
FT /note="S->A: 140-fold decrease in activity toward
FT salicylyl-CoA."
FT /evidence="ECO:0000269|PubMed:19193103"
FT MUTAGEN 67
FT /note="S->C: 104-fold decrease in activity toward
FT salicylyl-CoA."
FT /evidence="ECO:0000269|PubMed:19193103"
FT MUTAGEN 68
FT /note="M->A: 130-fold decrease in activity toward
FT salicylyl-CoA."
FT /evidence="ECO:0000269|PubMed:19193103"
FT MUTAGEN 68
FT /note="M->V: 47-fold increase in catalytic efficiency
FT toward 1,4-dihydroxy-2-naphthoyl-CoA and 10-fold increase
FT in catalytic efficiency toward lauroyl-CoA. Does not affect
FT catalytic efficiency toward benzoyl-CoA."
FT /evidence="ECO:0000269|PubMed:24992697,
FT ECO:0000269|PubMed:25010423"
FT HELIX 9..14
FT /evidence="ECO:0007829|PDB:4K4C"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:4K4C"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:4K4C"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:4K4C"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4K4C"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4K4C"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4K4C"
FT HELIX 55..71
FT /evidence="ECO:0007829|PDB:4K4C"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:4K4C"
FT STRAND 95..107
FT /evidence="ECO:0007829|PDB:4K4C"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:4K4C"
FT STRAND 125..136
FT /evidence="ECO:0007829|PDB:4K4C"
SQ SEQUENCE 137 AA; 14970 MW; C8DF8DE63815F206 CRC64;
MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF GLLHGGASAA
LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG VCQPLHLGRQ NQSWEIVVFD
EQGRRCCTCR LGTAVLG
