IROB_ECOL6
ID IROB_ECOL6 Reviewed; 371 AA.
AC A0A0H2V630;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Enterobactin C-glucosyltransferase {ECO:0000305};
DE Short=Ent C-glucosyltransferase {ECO:0000303|PubMed:15598734};
DE EC=2.4.1.369 {ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:24960592};
GN Name=iroB {ECO:0000303|PubMed:15598734};
GN OrderedLocusNames=c1254 {ECO:0000312|EMBL:AAN79728.1};
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 PATHWAY.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=15598734; DOI=10.1073/pnas.0408463102;
RA Fischbach M.A., Lin H., Liu D.R., Walsh C.T.;
RT "In vitro characterization of IroB, a pathogen-associated C-
RT glycosyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:571-576(2005).
RN [3]
RP FUNCTION.
RX PubMed=17163637; DOI=10.1021/cb0500034;
RA Luo M., Lin H., Fischbach M.A., Liu D.R., Walsh C.T., Groves J.T.;
RT "Enzymatic tailoring of enterobactin alters membrane partitioning and iron
RT acquisition.";
RL ACS Chem. Biol. 1:29-32(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 65-HIS-HIS-66; GLU-67; TRP-264 AND ASP-304.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=24960592; DOI=10.1016/j.bbapap.2014.06.010;
RA Foshag D., Campbell C., Pawelek P.D.;
RT "The C-glycosyltransferase IroB from pathogenic Escherichia coli:
RT identification of residues required for efficient catalysis.";
RL Biochim. Biophys. Acta 1844:1619-1630(2014).
CC -!- FUNCTION: Catalyzes the successive monoglucosylation, diglucosylation
CC and triglucosylation of enterobactin (Ent) (PubMed:15598734,
CC PubMed:24960592). Transfers glucosyl groups from uridine-5'-
CC diphosphoglucose (UDP-Glc) to C5 of one, two or three of the 2,3-
CC dihydroxybenzoyl (DHB) units of Ent to yield monoglucosyl-C-Ent (MGE),
CC diglucosyl-C-Ent (DGE) and triglucosyl-C-Ent (TGE) (PubMed:15598734,
CC PubMed:24960592). Glucosylation decreases the membrane affinity of Ent
CC and increases the iron acquisition rate (PubMed:17163637).
CC {ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:17163637,
CC ECO:0000269|PubMed:24960592}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=enterobactin + UDP-alpha-D-glucose = monoglucosyl-enterobactin
CC + UDP; Xref=Rhea:RHEA:24448, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:77805, ChEBI:CHEBI:142958; EC=2.4.1.369;
CC Evidence={ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:24960592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24449;
CC Evidence={ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:24960592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=monoglucosyl-enterobactin + UDP-alpha-D-glucose = diglucosyl-
CC enterobactin + H(+) + UDP; Xref=Rhea:RHEA:59096, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:142958,
CC ChEBI:CHEBI:142959; EC=2.4.1.369;
CC Evidence={ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:24960592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59097;
CC Evidence={ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:24960592};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diglucosyl-enterobactin + UDP-alpha-D-glucose = H(+) +
CC triglucosyl-enterobactin + UDP; Xref=Rhea:RHEA:59100,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885,
CC ChEBI:CHEBI:142959, ChEBI:CHEBI:142960; EC=2.4.1.369;
CC Evidence={ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:24960592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59101;
CC Evidence={ECO:0000269|PubMed:15598734, ECO:0000269|PubMed:24960592};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.2 uM for enterobactin {ECO:0000269|PubMed:15598734};
CC KM=13.3 uM for UDP-Glc (for the first C-glucosylation)
CC {ECO:0000269|PubMed:15598734};
CC Note=kcat is 11.2 min(-1) with enterobactin as substrate. kcat is 9.7
CC min(-1) with UDP-Glc as substrate (for the first C-glucosylation).
CC {ECO:0000269|PubMed:15598734};
CC -!- PATHWAY: Siderophore biosynthesis; enterobactin biosynthesis.
CC {ECO:0000269|PubMed:15598734}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:24960592}. Note=May
CC associate with the inner membrane via hydrophobic and electrostatic
CC interactions. {ECO:0000305|PubMed:24960592}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN79728.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN79728.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001221122.1; NZ_CP051263.1.
DR AlphaFoldDB; A0A0H2V630; -.
DR SMR; A0A0H2V630; -.
DR STRING; 199310.c1254; -.
DR EnsemblBacteria; AAN79728; AAN79728; c1254.
DR KEGG; ecc:c1254; -.
DR eggNOG; COG1819; Bacteria.
DR HOGENOM; CLU_000537_7_4_6; -.
DR BioCyc; MetaCyc:MON-20653; -.
DR BRENDA; 2.4.1.369; 16864.
DR UniPathway; UPA00017; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009239; P:enterobactin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR010610; DUF1205.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF06722; DUF1205; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Enterobactin biosynthesis; Glycosyltransferase; Transferase.
FT CHAIN 1..371
FT /note="Enterobactin C-glucosyltransferase"
FT /id="PRO_0000452107"
FT MUTAGEN 65..66
FT /note="HH->AA: Converts 92% of Ent to MGE (60%) and DGE
FT (32%)."
FT /evidence="ECO:0000269|PubMed:24960592"
FT MUTAGEN 67
FT /note="E->A: Converts 29% of Ent to MGE."
FT /evidence="ECO:0000269|PubMed:24960592"
FT MUTAGEN 264
FT /note="W->L: Convert 55% of Ent to MGE (45%) and DGE
FT (10%)."
FT /evidence="ECO:0000269|PubMed:24960592"
FT MUTAGEN 304
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24960592"
SQ SEQUENCE 371 AA; 40292 MW; D3D07B0D71854DEA CRC64;
MRILFVGPPL YGLLYPVLSL AQAFRVNGHE VLIASGGQFA QKAAEAGLVV FDAAPGLDSE
AGYRHHEAQR KKSNIGTQMG NFSFFSEEMA DHLVEFAGHW RPDLIIYPPL GVIGPLIAAK
YDIPVVMQTV GFGHTPWHIR GVTRSLTDAY RRHNVGATPR DMAWIDVTPP SMSILENDGE
PIIPMQYVPY NGGAVWEPWW ERRPDRKRLL VSLGTVKPMV DGLDLIAWVM DSASEVDAEI
ILHISANARS DLRSLPSNVR LVDWIPMGVF LNGADGFIHH GGAGNTLTAL HAGIPQIVFG
QGADRPVNAR VVAERGCGII PGDVGLSSNM INAFLNNRSL RKASEEVAAE MAAQPCPGEV
AKSLITMVQK G
