ISLA_BILW3
ID ISLA_BILW3 Reviewed; 830 AA.
AC E5Y378;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Isethionate sulfite-lyase {ECO:0000303|PubMed:30718429};
DE EC=4.4.1.- {ECO:0000269|PubMed:30718429};
DE AltName: Full=Glycyl radical enzyme IslA {ECO:0000303|PubMed:30718429};
DE Short=GRE IslA {ECO:0000303|PubMed:30718429};
GN Name=islA {ECO:0000303|PubMed:30718429}; Synonyms=iseG;
GN ORFNames=HMPREF0179_00639 {ECO:0000312|EMBL:EFV45544.1};
OS Bilophila wadsworthia (strain 3_1_6).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Bilophila.
OX NCBI_TaxID=563192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_6;
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Sibley C., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bilophila wadsworthia 3_1_6.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, INDUCTION, AND PATHWAY.
RC STRAIN=3_1_6;
RX PubMed=30718429; DOI=10.1073/pnas.1815661116;
RA Peck S.C., Denger K., Burrichter A., Irwin S.M., Balskus E.P.,
RA Schleheck D.;
RT "A glycyl radical enzyme enables hydrogen sulfide production by the human
RT intestinal bacterium Bilophila wadsworthia.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:3171-3176(2019).
CC -!- FUNCTION: Involved in an anaerobic respiration pathway that converts
CC the sulfonate taurine (2-aminoethanesulfonate) to ammonia, acetate and
CC sulfide. Catalyzes the radical-mediated C-S bond cleavage of
CC isethionate (2-hydroxyethanesulfonate) to form sulfite and
CC acetaldehyde. Is not able to use any alternate organosulfonate or (S)-
CC 1,2-propanediol or choline as a substrate, showing that this enzyme is
CC highly specific for isethionate. {ECO:0000269|PubMed:30718429}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyethane-1-sulfonate = acetaldehyde + H(+) + sulfite;
CC Xref=Rhea:RHEA:60452, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:61904;
CC Evidence={ECO:0000269|PubMed:30718429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60453;
CC Evidence={ECO:0000305|PubMed:30718429};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.1 mM for 2-hydroxyethane-1-sulfonate
CC {ECO:0000269|PubMed:30718429};
CC Note=kcat is 14 sec(-1). {ECO:0000269|PubMed:30718429};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000305|PubMed:30718429}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q727N1}.
CC -!- INDUCTION: Highly up-regulated in the presence of taurine or
CC isethionate. {ECO:0000269|PubMed:30718429}.
CC -!- PTM: Requires the activating protein IslB to generate the key active
CC site glycyl radical on Gly-805 that is involved in catalysis.
CC {ECO:0000269|PubMed:30718429}.
CC -!- MISCELLANEOUS: Taurine is an abundant dietary and host-derived molecule
CC whose metabolism to hydrogen sulfide (H2S) by members of the human gut
CC microbiota has many prominent connections to host health and disease.
CC The human gut bacterium and opportunistic pathogen Bilophila
CC wadsworthia produces H2S when respiring sulfite (HSO3-) released from
CC organosulfonate substrates such as taurine and isethionate.
CC {ECO:0000305|PubMed:30718429}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family.
CC {ECO:0000305}.
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DR EMBL; ADCP02000001; EFV45544.1; -; Genomic_DNA.
DR RefSeq; WP_005024906.1; NZ_KE150238.1.
DR PDB; 7KQ3; X-ray; 2.69 A; A/B/C/D=1-830.
DR PDB; 7KQ4; X-ray; 2.26 A; A/B=1-830.
DR PDBsum; 7KQ3; -.
DR PDBsum; 7KQ4; -.
DR AlphaFoldDB; E5Y378; -.
DR SMR; E5Y378; -.
DR STRING; 563192.HMPREF0179_00639; -.
DR EnsemblBacteria; EFV45544; EFV45544; HMPREF0179_00639.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_009096_0_1_7; -.
DR BioCyc; MetaCyc:MON-20851; -.
DR BRENDA; 4.4.1.38; 856.
DR UniPathway; UPA00338; -.
DR Proteomes; UP000006034; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR019777; Form_AcTrfase_GR_CS.
DR InterPro; IPR001150; Gly_radical.
DR InterPro; IPR004184; PFL_dom.
DR Pfam; PF01228; Gly_radical; 1.
DR Pfam; PF02901; PFL-like; 1.
DR PROSITE; PS00850; GLY_RADICAL_1; 1.
DR PROSITE; PS51149; GLY_RADICAL_2; 1.
DR PROSITE; PS51554; PFL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Organic radical; Reference proteome.
FT CHAIN 1..830
FT /note="Isethionate sulfite-lyase"
FT /id="PRO_0000450941"
FT DOMAIN 31..700
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 707..830
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT ACT_SITE 468
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q30W70"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q30W70"
FT BINDING 189
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT BINDING 193
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT BINDING 468..470
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT BINDING 678
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT MOD_RES 805
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 31..37
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 38..42
FT /evidence="ECO:0007829|PDB:7KQ3"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7KQ3"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 198..219
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 231..262
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 290..307
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 338..354
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 376..382
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 392..403
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 421..431
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 443..452
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 474..476
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 488..496
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:7KQ3"
FT HELIX 522..551
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 552..554
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 558..562
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 565..570
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 585..591
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 593..606
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 615..623
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 624..628
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 630..636
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 647..667
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 673..679
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 682..684
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 685..690
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 721..729
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 738..741
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 744..747
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 750..752
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 754..770
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 775..780
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 783..791
FT /evidence="ECO:0007829|PDB:7KQ4"
FT TURN 793..798
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 804..809
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 810..812
FT /evidence="ECO:0007829|PDB:7KQ4"
FT HELIX 815..823
FT /evidence="ECO:0007829|PDB:7KQ4"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:7KQ4"
SQ SEQUENCE 830 AA; 93965 MW; A0F49549EB008727 CRC64;
MTQVAEIKSP HEQRLEDNIA GKEDIYRESH KRVFKLLERF DGQKPAIDVE RALYFTQSMA
ETVGQPLVLR WAKALMNVAK NITVMVQDDQ LLLGRCGGHD GRYGILYPEL DGDFLDIAVR
DLPTRPQSPA SISPEDAKIV VEQIAPFWKG RTYHEALNKA LPAEVHKLTY DDPDGLISRF
IVNETSSFRS SIQWVHDYEV VLKRGFNGLK QEMEEKLAAL DPASPVDQVD KRPFIEATIL
VCDAIVLWAK RHADAARKAA EACADPVRKA ELIRMAENAE HVPANPARDF YEAVQSQYFT
QMFSRLEQKT GTTISNGRMD QYFYPFYKKD MEAGILTDEK TLEYLECMWV GMAEFIDMYI
SPAGGAFNEG YAHWEAVTIG GQTPDGRDAT NDLTYLFLKS KREFPLHYPD LAARIHSRAP
ERYLWDVAET IKFGSGFPKL CNDEECIPLY VSKGATFEEA LDYAVSGCIE IRMPNRDTYT
SGGAYTNFAS AVEMALYDGK MKKYGDVQLG IQTGDARKFK SWDEFWNAYV QQHMLLLRTT
FIQQYIVIQT RAKHFAQPMG SVLHALCRKH CIDLHQPQIP EGLNFGYFEF MGLGTVIDSL
AAIKKLVFED KKLTMDQLID ALEANFEGYE DIQQLLRTAP CYGNDDEYAD EIGRELDRMA
VSFAAKYGKE MGINNDARYV PFTSHVPFGK VVSATPNGRV AWFPLADGSS PSHGADHNGP
TAILLSNHNT KNYGMRARAA RLINVKFTPK CVEGDAGTEK LVQFIRTWCD LKLWHIQFNV
INADTLKKAQ KDPQKYRNLI VRIAGYSAYF VDLTPDLQND LIARTGHDQM
