IROD_ECOL6
ID IROD_ECOL6 Reviewed; 409 AA.
AC A0A0H2V660;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Iron(III) salmochelin esterase {ECO:0000305};
DE EC=3.1.1.109 {ECO:0000269|PubMed:16076215};
GN Name=iroD {ECO:0000303|PubMed:16076215};
GN OrderedLocusNames=c1252 {ECO:0000312|EMBL:AAN79709.1};
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=16076215; DOI=10.1021/ja0522027;
RA Lin H., Fischbach M.A., Liu D.R., Walsh C.T.;
RT "In vitro characterization of salmochelin and enterobactin trilactone
RT hydrolases IroD, IroE, and Fes.";
RL J. Am. Chem. Soc. 127:11075-11084(2005).
CC -!- FUNCTION: Catalyzes the hydrolysis of both the apo and Fe3(+)-bound
CC forms of enterobactin (Ent), monoglucosyl-C-Ent (MGE), diglucosyl-C-Ent
CC (DGE) and triglucosyl-C-Ent (TGE). Shows higher catalytic efficiencies
CC on Fe3(+)-bound forms. The initial linear trimer products are, in turn,
CC very good substrates for further hydrolytic cleavage by IroD, leading
CC to complete degradation of the trilactone to DHB-Ser and/or Glc-DHB-Ser
CC monomers. Hydrolyzes MGE and DGE regioselectively. May be the ferric
CC MGE/DGE esterase responsible for cytoplasmic iron release.
CC {ECO:0000269|PubMed:16076215}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-C-5-deoxy-beta-D-glucosyl-enterobactin + H2O =
CC Fe(III)-{di[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-[deoxy-beta-D-
CC glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + H(+);
CC Xref=Rhea:RHEA:60392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:143772, ChEBI:CHEBI:143774; EC=3.1.1.109;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-{di[N-(2,3-dihydroxybenzoyl)-L-seryl]-N-(C-5-[deoxy-
CC beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + H(+) + H2O =
CC Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-N-(C-5-[deoxy-beta-D-
CC glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + N-(2,3-dihydroxybenzoyl)-
CC L-serine; Xref=Rhea:RHEA:60404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58154, ChEBI:CHEBI:143774, ChEBI:CHEBI:143775;
CC EC=3.1.1.109; Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-
CC D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+) + H2O =
CC Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-N-(C-5-[deoxy-beta-D-
CC glucosyl]-2,3-dihydroxybenzoyl)-L-serine} + N-(C-5-[deoxy-beta-D-
CC glucosyl]-2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:60400,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:143773,
CC ChEBI:CHEBI:143775, ChEBI:CHEBI:143778; EC=3.1.1.109;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-di(C-5-deoxy-beta-D-glucosyl)-enterobactin + H2O =
CC Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-D-
CC glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+);
CC Xref=Rhea:RHEA:60388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:143771, ChEBI:CHEBI:143773; EC=3.1.1.109;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-{N-(2,3-dihydroxybenzoyl)-L-seryl-[N-(C-5-[deoxy-beta-
CC D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2} + H(+) + H2O = Fe(III)-
CC [N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-L-serine]2 + N-
CC (2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:60396,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58154,
CC ChEBI:CHEBI:143773, ChEBI:CHEBI:143776; EC=3.1.1.109;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-2,3-dihydroxybenzoyl)-
CC L-serine]2 + H(+) + H2O = Fe(III)-[N-(C-5-[deoxy-beta-D-glucosyl]-
CC 2,3-dihydroxybenzoyl)-L-serine] + N-(C-5-[deoxy-beta-D-glucosyl]-2,3-
CC dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:60408, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:143776, ChEBI:CHEBI:143777,
CC ChEBI:CHEBI:143778; EC=3.1.1.109;
CC Evidence={ECO:0000269|PubMed:16076215};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for Ent {ECO:0000269|PubMed:16076215};
CC KM=0.12 uM for Fe-Ent {ECO:0000269|PubMed:16076215};
CC KM=60 uM for MGE {ECO:0000269|PubMed:16076215};
CC KM=0.08 uM for Fe-MGE {ECO:0000269|PubMed:16076215};
CC KM=120 uM for DGE {ECO:0000269|PubMed:16076215};
CC KM=0.12 uM for Fe-DGE {ECO:0000269|PubMed:16076215};
CC KM=160 uM for TGE {ECO:0000269|PubMed:16076215};
CC KM=0.43 uM for Fe-TGE {ECO:0000269|PubMed:16076215};
CC Note=kcat is 1060 min(-1) with Ent as substrate. kcat is 74 min(-1)
CC with Fe-Ent as substrate. kcat is 3720 min(-1) with MGE as substrate.
CC kcat is 46 min(-1) with Fe-MGE as substrate. kcat is 6500 min(-1)
CC with DGE as substrate. kcat is 32 min(-1) with Fe-DGE as substrate.
CC kcat is 4460 min(-1) with TGE as substrate. kcat is 84 min(-1) with
CC Fe-TGE as substrate. {ECO:0000269|PubMed:16076215};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:16076215}.
CC -!- SIMILARITY: Belongs to the Fes family. {ECO:0000305}.
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DR EMBL; AE014075; AAN79709.1; -; Genomic_DNA.
DR RefSeq; WP_000933673.1; NC_004431.1.
DR AlphaFoldDB; A0A0H2V660; -.
DR SMR; A0A0H2V660; -.
DR STRING; 199310.c1252; -.
DR EnsemblBacteria; AAN79709; AAN79709; c1252.
DR KEGG; ecc:c1252; -.
DR eggNOG; COG2382; Bacteria.
DR HOGENOM; CLU_024314_3_0_6; -.
DR OMA; GSYWWAP; -.
DR BioCyc; MetaCyc:MON-20652; -.
DR BRENDA; 3.1.1.109; 2026.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008849; F:enterochelin esterase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR021764; Enterochelin_esterase_N.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF11806; DUF3327; 1.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..409
FT /note="Iron(III) salmochelin esterase"
FT /id="PRO_0000452106"
SQ SEQUENCE 409 AA; 44760 MW; E4847E21702B3E76 CRC64;
MLNMQQHPSA IASLRNQLAA GHIANLTDFW REAESLNVPL VTPVEGAEDE REVTFLWRAR
HPLQGVYLRL NRVTDKEHVE KGMMSALPET DIWTLTLRLP ASYCGSYSLL EIPPGTTAET
IALSGGRFAT LAGKADPLNK MPEINVRGNA KESVLTLDKA PALSEWNGGF HTGQLLTSMR
IIAGKSRQVR LYIPDIDISQ PLGLVVLPDG ETWFDHLGVC AAIDAAINNR RIVPVAVLGI
DNINEHERTE ILGGRSKLIK DIAGHLLPMI RAEQPQRQWA DRSRTVLAGQ SLGGISALMG
ARYAPETFGL VLSHSPSMWW TPERTSRPGL FSETDTSWVS EHLLSAPPQG VRISLCVGSL
EGSTVPHVQQ LHQRLITAGV ESHCAIYTGG HDYAWWRGAL IDGIGLLQG
