ISLA_OLEA2
ID ISLA_OLEA2 Reviewed; 829 AA.
AC Q312S2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Isethionate sulfite-lyase {ECO:0000303|PubMed:30718429};
DE EC=4.4.1.- {ECO:0000250|UniProtKB:B8J0R1, ECO:0000305|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};
GN OrderedLocusNames=Dde_1273 {ECO:0000312|EMBL:ABB38074.1};
OS Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS (Desulfovibrio alaskensis).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Oleidesulfovibrio.
OX NCBI_TaxID=207559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX PubMed=21685289; DOI=10.1128/jb.05400-11;
RA Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT "Complete genome sequence and updated annotation of Desulfovibrio
RT alaskensis G20.";
RL J. Bacteriol. 193:4268-4269(2011).
RN [2]
RP FUNCTION, INDUCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
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 isethionate (2-hydroxyethanesulfonate) to ammonia,
CC acetate and sulfide. Catalyzes the radical-mediated C-S bond cleavage
CC of isethionate (2-hydroxyethanesulfonate) to form sulfite and
CC acetaldehyde. {ECO:0000305|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:0000250|UniProtKB:B8J0R1, ECO:0000305|PubMed:30718429};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60453;
CC Evidence={ECO:0000269|PubMed:30718429};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000269|PubMed:30718429}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q727N1}.
CC -!- INDUCTION: Highly up-regulated in the presence of isethionate.
CC {ECO:0000269|PubMed:30718429}.
CC -!- PTM: Requires the activating protein IslB to generate the key active
CC site glycyl radical on Gly-804 that is involved in catalysis.
CC {ECO:0000250|UniProtKB:B8J0R1}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC with isethionate as the terminal electron acceptor.
CC {ECO:0000269|PubMed:30718429}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family.
CC {ECO:0000305}.
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DR EMBL; CP000112; ABB38074.1; -; Genomic_DNA.
DR RefSeq; WP_011367272.1; NC_007519.1.
DR AlphaFoldDB; Q312S2; -.
DR SMR; Q312S2; -.
DR STRING; 207559.Dde_1273; -.
DR EnsemblBacteria; ABB38074; ABB38074; Dde_1273.
DR KEGG; dde:Dde_1273; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_009096_0_1_7; -.
DR OMA; HVQYNIV; -.
DR OrthoDB; 116406at2; -.
DR UniPathway; UPA00338; -.
DR Proteomes; UP000002710; Chromosome.
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 2: Evidence at transcript level;
KW Lyase; Organic radical; Pyruvate; Reference proteome.
FT CHAIN 1..829
FT /note="Isethionate sulfite-lyase"
FT /id="PRO_0000450942"
FT DOMAIN 31..699
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 706..829
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT ACT_SITE 467
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q30W70"
FT ACT_SITE 469
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q30W70"
FT BINDING 188
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT BINDING 192
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT BINDING 467..469
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT BINDING 677
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT MOD_RES 804
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 829 AA; 94135 MW; 3259CAE3A49AE8BB CRC64;
MQCCTTPLSP HEQRLQDKIA GKEDSFRKSH ERVFNILDSF DGKRPRIDVE RAKLFTDSMK
ETEGQPLVLR WAKAMKHVAE HITVYIDDDQ LICGRGGCPG RYGVLYPELD GDFLDLAIED
LPNRTESPFT ITEADARVVV EEIAPYWKGK TYHEDLNLAL PSDVHKLTYD DPQGLKSRFI
VNETSSFRSS IQWVHDYEKV LKRGFRGLKE EAQEKIAGLD PLSPRDNVEK RPFLEAIVIV
CDAIILWANR HAKLAADMAA AETNPVRKAE LETMAEICAW VPENPARNFY EAVQAQWFTQ
MFSRLEQKTG TIVSNGRMDQ YFWPFYRKDI EEGRITEESA LELLECMWVG MAQYVDLYIS
PAGGAFNEGY AHWEAVTIGG QTPQGLDATN DLTYLFLKSK REFPLHYPDL AARIHSRSPE
RYLHDVAETI KFGSGFPKLI NDEEIVPLYV SKGASFEEAL DYAVSGCTEA RMPNRDTYTS
GGAYINFAAA LEMVLYNGRM LKYGENELGL ETGDPTRFET WEEFWNAYVL QHEHFLRAAF
IQQHIINNVR ARHFAQPMGS ALHDLCMKHC LDLHTPQIPE GINLGYFEYM GFGTVVDSLA
AIKKLVFEDK KLTMQEVIEA LKCNFEGKED VQQMLKSAPC YGNNDEYADS IAREIDAISV
KYGRRYSPEL GMHNDVRYVP FTSHVPFGKV VSATPNGRLA WTPLSDGSSA SHGADVNGPT
AVLQSNFSSK NYGYRDRAAR MLNIKFTPKC VEGDEGTEKL VSFIRTFCDL KLWHVQFNVI
NRDTLIAAQK DPEKYRSLIV RIAGYSAYFV DLSPDLQNDL IARTQHDAM
