ISLA_DESDA
ID ISLA_DESDA Reviewed; 831 AA.
AC B8J0R1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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};
GN OrderedLocusNames=Ddes_1436 {ECO:0000312|EMBL:ACL49338.1};
OS Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=525146;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27774 / DSM 6949 / MB;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Hazen T.C.;
RT "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT ATCC 27774.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND
RP PATHWAY.
RC STRAIN=DSM 642;
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: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=6.3 mM for 2-hydroxyethane-1-sulfonate
CC {ECO:0000269|PubMed:30718429};
CC Note=kcat is 12 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 isethionate.
CC {ECO:0000269|PubMed:30718429}.
CC -!- PTM: Requires the activating protein IslB to generate the key active
CC site glycyl radical on Gly-806 that is involved in catalysis.
CC {ECO:0000269|PubMed:30718429}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family.
CC {ECO:0000305}.
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DR EMBL; CP001358; ACL49338.1; -; Genomic_DNA.
DR AlphaFoldDB; B8J0R1; -.
DR SMR; B8J0R1; -.
DR STRING; 525146.Ddes_1436; -.
DR EnsemblBacteria; ACL49338; ACL49338; Ddes_1436.
DR KEGG; dds:Ddes_1436; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_009096_0_1_7; -.
DR OMA; HVQYNIV; -.
DR BRENDA; 4.4.1.38; 1905.
DR UniPathway; UPA00338; -.
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 Lyase; Organic radical; Pyruvate.
FT CHAIN 1..831
FT /note="Isethionate sulfite-lyase"
FT /id="PRO_0000450943"
FT DOMAIN 32..701
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 708..831
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 679
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000250|UniProtKB:Q727N1"
FT MOD_RES 806
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
SQ SEQUENCE 831 AA; 94548 MW; F586F47BE0512A1A CRC64;
MSMTTCECRS PQEQRLYDKI EGREDRFRKT HPRVFRLLER FEGQKPRIDI ERALYFTQSM
QETEGQPLVL RWAKALMHIA RNMTVYVQED QLLLGRAGCD GRYGILYPEL DGDFLDIAVR
DLPTRKTSPA TITPEDARRV VEEIAPYWKG KTYHEALNAA LPAEVHKLTY DDPEGLISRF
IVNETSSFRS SIQWVHDYEK ILKRGFNSIK KEAREKLAAL DPLSAKDDRE KRPFLEAVMI
VCDAIVLWAK RHAVLAREMA EKESDPVRKA ELLRMAENAE HVPGEPARDF WEACQSQWFT
QMFSRIEQKT GTTISNGRMD QYFQPYYKQD REAGKITEAQ AMELLECMWV GMAEFIDMYI
SPTGGAFNEG YAHWEAVTVG GQTPDGRDAS NDLTYLILKS KREFPLHYPD LAARIHSRAP
ERYLWDVAET IKYGSGFPKL INDEEIVPLY VSKGATFEEA LDYAVSGCTE ARMPNRDTYT
SGGAYINFAA AVEMVLRNGR MKKYGDQKLG VETGDPRSFT TWDQFWNAYV EQHLLFLKTA
FTQQYIINKL RAEHFAQPMG SAMHDLCMKH CIDLHQEQIP EGINLGYFEY MGLGTVVDSL
AAVKKLVFEE KKLSMDKLIA AIDADFEGYE DVRALLRSAP CYGNNDEYAD AIGRDIDRIS
VEYGNKYSMS DLGIHNDVRY VPFTSHVPFG KVVSATPNGR TDGFPLSDGS SASHGADVNG
PTAVLLSNCT TKNMGLRDRA ARMLNIKFTP KCVEGEQGTE KLVSFIRTFC DLKLWHVQFN
VVNKGTLVAA QKDPQKYRNL IVRIAGYSAY FVDLSPDLQN DLIARTEHDV M
