ASST_ECOL6
ID ASST_ECOL6 Reviewed; 598 AA.
AC Q8FDI4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Arylsulfate sulfotransferase AssT {ECO:0000255|HAMAP-Rule:MF_00933};
DE EC=2.8.2.22 {ECO:0000255|HAMAP-Rule:MF_00933};
DE AltName: Full=Aryl sulfotransferase AssT {ECO:0000255|HAMAP-Rule:MF_00933};
DE Flags: Precursor;
GN Name=assT {ECO:0000255|HAMAP-Rule:MF_00933}; OrderedLocusNames=c3785;
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 PARTIAL PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY
RP MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=18565543; DOI=10.1016/j.jmb.2008.05.031;
RA Grimshaw J.P., Stirnimann C.U., Brozzo M.S., Malojcic G., Grutter M.G.,
RA Capitani G., Glockshuber R.;
RT "DsbL and DsbI form a specific dithiol oxidase system for periplasmic
RT arylsulfate sulfotransferase in uropathogenic Escherichia coli.";
RL J. Mol. Biol. 380:667-680(2008).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 28-598 IN COMPLEXES WITH
RP P-NITROPHENOL AND 4-METHYLUMBELLIFERYLSULFATE, PARTIAL PROTEIN SEQUENCE OF
RP N-TERMINUS, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BOND,
RP BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY,
RP MUTAGENESIS OF TYR-123; TYR-235; HIS-279; HIS-383; ARG-401 AND TYR-586, AND
RP ACTIVE SITE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=19036922; DOI=10.1073/pnas.0806997105;
RA Malojcic G., Owen R.L., Grimshaw J.P., Brozzo M.S., Dreher-Teo H.,
RA Glockshuber R.;
RT "A structural and biochemical basis for PAPS-independent sulfuryl transfer
RT by aryl sulfotransferase from uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19217-19222(2008).
CC -!- FUNCTION: Catalyzes the transfer of sulfuryl groups between phenolic
CC compounds. {ECO:0000255|HAMAP-Rule:MF_00933,
CC ECO:0000269|PubMed:18565543, ECO:0000269|PubMed:19036922}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phenol + an aryl sulfate = a phenol + an aryl sulfate;
CC Xref=Rhea:RHEA:51072, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317;
CC EC=2.8.2.22; Evidence={ECO:0000255|HAMAP-Rule:MF_00933,
CC ECO:0000269|PubMed:18565543, ECO:0000269|PubMed:19036922};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.35 mM for phenol {ECO:0000269|PubMed:19036922};
CC KM=45 uM for 4-methylumbelliferylsulfate
CC {ECO:0000269|PubMed:19036922};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18565543,
CC ECO:0000269|PubMed:19036922}.
CC -!- INTERACTION:
CC Q8FDI4; Q8FDI4: assT; NbExp=2; IntAct=EBI-15743267, EBI-15743267;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:18565543}.
CC -!- INDUCTION: Expressed from a tri-cistronic operon that encodes AssT,
CC DsbI and DsbL. {ECO:0000269|PubMed:18565543}.
CC -!- PTM: The disulfide bond is crucial for enzyme activity.
CC {ECO:0000269|PubMed:19036922}.
CC -!- MISCELLANEOUS: Most commensal E.coli strains do not have a gene for
CC arylsulfate sulfotransferase, in contrast to strain CFT073 and other
CC uropathogenic strains. {ECO:0000305|PubMed:19036922}.
CC -!- SIMILARITY: Belongs to the aryl sulfotransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_00933}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN82229.1; -; Genomic_DNA.
DR RefSeq; WP_000459868.1; NC_004431.1.
DR PDB; 3ELQ; X-ray; 2.00 A; A/B=28-598.
DR PDB; 3ETS; X-ray; 2.40 A; A/B=28-598.
DR PDB; 3ETT; X-ray; 2.10 A; A/B=28-598.
DR PDBsum; 3ELQ; -.
DR PDBsum; 3ETS; -.
DR PDBsum; 3ETT; -.
DR SMR; Q8FDI4; -.
DR STRING; 199310.c3785; -.
DR EnsemblBacteria; AAN82229; AAN82229; c3785.
DR KEGG; ecc:c3785; -.
DR eggNOG; ENOG502ZAQ1; Bacteria.
DR HOGENOM; CLU_026635_2_0_6; -.
DR OMA; PANCYRA; -.
DR BioCyc; ECOL199310:C3785-MON; -.
DR BRENDA; 2.8.2.22; 2026.
DR SABIO-RK; Q8FDI4; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004062; F:aryl sulfotransferase activity; IEA:InterPro.
DR GO; GO:0047686; F:arylsulfate sulfotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 2.60.40.3100; -; 1.
DR HAMAP; MF_00933; Arylsulfotrans_AssT; 1.
DR InterPro; IPR035391; Arylsulfotran_N.
DR InterPro; IPR010262; Arylsulfotransferase_bact.
DR InterPro; IPR028610; AssT_Enterobac.
DR InterPro; IPR038477; ASST_N_sf.
DR Pfam; PF17425; Arylsulfotran_N; 1.
DR Pfam; PF05935; Arylsulfotrans; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm; Signal;
KW Transferase.
FT SIGNAL 1..27
FT CHAIN 28..598
FT /note="Arylsulfate sulfotransferase AssT"
FT /id="PRO_0000418844"
FT ACT_SITE 463
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00933,
FT ECO:0000269|PubMed:19036922"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00933,
FT ECO:0000305|PubMed:19036922"
FT BINDING 383
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00933,
FT ECO:0000305|PubMed:19036922"
FT DISULFID 445..451
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00933,
FT ECO:0000269|PubMed:19036922"
FT MUTAGEN 123
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:19036922"
FT MUTAGEN 235
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:19036922"
FT MUTAGEN 279
FT /note="H->L: Reduces enzyme activity by 96%."
FT /evidence="ECO:0000269|PubMed:19036922"
FT MUTAGEN 383
FT /note="H->L: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:19036922"
FT MUTAGEN 401
FT /note="R->L: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:19036922"
FT MUTAGEN 586
FT /note="Y->F: Reduces enzyme activity by about 40%."
FT /evidence="ECO:0000269|PubMed:19036922"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 104..114
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 289..295
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3ETS"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:3ELQ"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:3ELQ"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 496..503
FT /evidence="ECO:0007829|PDB:3ELQ"
FT TURN 504..507
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 508..515
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 517..523
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:3ELQ"
FT TURN 535..538
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 539..547
FT /evidence="ECO:0007829|PDB:3ELQ"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 557..564
FT /evidence="ECO:0007829|PDB:3ELQ"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 570..577
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:3ELQ"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:3ELQ"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:3ELQ"
SQ SEQUENCE 598 AA; 66570 MW; 309EE9E1580D7FB0 CRC64;
MFDKYRKTLV AGTVAITLGL SASGVMAAGF KPAPPAGQLG AVIVDPYGNA PLTALVDLDS
HVISDVKVTV HGKGEKGVEI SYPVGQESLK TYDGVPIFGL YQKFANKVTV EWKENGKVMK
DDYVVHTSAI VNNYMDNRSI SDLQQTKVIK VAPGFEDRLY LVNTHTFTAQ GXDLHWHGEK
DKNAGILDAG PATGALPFDI APFTFIVDTE GEYRWWLDQD TFYDGRDRDI NKRGYLMGIR
ETPRGTFTAV QGQHWYEFDM MGQVLEDHKL PRGFADATHE SIETPNGTVL LRVGKSNYRR
DDGVHVTTIR DHILEVDKSG RVVDVWDLTK ILDPKRDALL GALDAGAVCV NVDLAHAGQQ
AKLEPDTPFG DALGVGPGRN WAHVNSIAYD AKDDSIILSS RHQGVVKIGR DKQVKWILAP
SKGWEKPLAS KLLKPVDANG KPITCNENGL CENSDFDFTY TQHTAWISSK GTLTIFDNGD
GRHLEQPALP TMKYSRFVEY KIDEKKGTVQ QVWEYGKERG YDFYSPITSI IEYQADRNTM
FGFGGSIHLF DVGQPTVGKL NEIDYKTKEV KVEIDVLSDK PNQTHYRALL VRPQQMFK
