ISLA_DESVH
ID ISLA_DESVH Reviewed; 828 AA.
AC Q727N1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Isethionate sulfite-lyase {ECO:0000303|PubMed:30962433};
DE EC=4.4.1.- {ECO:0000269|PubMed:30962433};
DE AltName: Full=C-S lyase IseG {ECO:0000303|PubMed:30962433};
DE AltName: Full=Glycyl radical enzyme IseG {ECO:0000303|PubMed:30962433};
DE Short=GRE IseG {ECO:0000303|PubMed:30962433};
GN Name=iseG {ECO:0000303|PubMed:30962433};
GN OrderedLocusNames=DVU_2824 {ECO:0000312|EMBL:AAS97296.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [2] {ECO:0007744|PDB:5YMR}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 24-828 IN COMPLEX WITH
RP 2-HYDROXYETHANESULFONATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT, PATHWAY, REACTION MECHANISM,
RP AND ACTIVE SITE.
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=30962433; DOI=10.1038/s41467-019-09618-8;
RA Xing M., Wei Y., Zhou Y., Zhang J., Lin L., Hu Y., Hua G., Urs A.N.N.,
RA Liu D., Wang F., Guo C., Tong Y., Li M., Liu Y., Ang E.L., Zhao H.,
RA Yuchi Z., Zhang Y.;
RT "Radical-mediated C-S bond cleavage in C2 sulfonate degradation by
RT anaerobic bacteria.";
RL Nat. Commun. 10:1609-1609(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. Shows no activity with taurine or ethanolamine as
CC substrates. {ECO:0000269|PubMed:30962433}.
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:30962433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60453;
CC Evidence={ECO:0000305|PubMed:30962433};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44.8 mM for 2-hydroxyethane-1-sulfonate
CC {ECO:0000269|PubMed:30962433};
CC Note=kcat is 91.6 sec(-1). {ECO:0000269|PubMed:30962433};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000305|PubMed:30962433}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30962433}.
CC -!- PTM: Requires the activating protein IseH to generate the key active
CC site glycyl radical on Gly-803 that is involved in catalysis.
CC {ECO:0000269|PubMed:30962433}.
CC -!- SIMILARITY: Belongs to the glycyl radical enzyme (GRE) family.
CC {ECO:0000305}.
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DR EMBL; AE017285; AAS97296.1; -; Genomic_DNA.
DR RefSeq; WP_010940090.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_012036.1; NC_002937.3.
DR PDB; 5YMR; X-ray; 2.40 A; A/B/C/D=24-828.
DR PDBsum; 5YMR; -.
DR AlphaFoldDB; Q727N1; -.
DR SMR; Q727N1; -.
DR STRING; 882.DVU_2824; -.
DR PaxDb; Q727N1; -.
DR EnsemblBacteria; AAS97296; AAS97296; DVU_2824.
DR KEGG; dvu:DVU_2824; -.
DR PATRIC; fig|882.5.peg.2552; -.
DR eggNOG; COG1882; Bacteria.
DR HOGENOM; CLU_009096_0_1_7; -.
DR OMA; KGWGQPA; -.
DR PhylomeDB; Q727N1; -.
DR BRENDA; 4.4.1.38; 1914.
DR UniPathway; UPA00338; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase 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; Pyruvate; Reference proteome;
KW Transferase.
FT CHAIN 1..828
FT /note="Isethionate sulfite-lyase"
FT /id="PRO_0000450944"
FT DOMAIN 30..698
FT /note="PFL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00887"
FT DOMAIN 705..828
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT ACT_SITE 466
FT /note="Cysteine radical intermediate"
FT /evidence="ECO:0000305|PubMed:30962433"
FT ACT_SITE 468
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:30962433"
FT BINDING 187
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000269|PubMed:30962433"
FT BINDING 191
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000269|PubMed:30962433"
FT BINDING 466..468
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000269|PubMed:30962433"
FT BINDING 676
FT /ligand="2-hydroxyethane-1-sulfonate"
FT /ligand_id="ChEBI:CHEBI:61904"
FT /evidence="ECO:0000269|PubMed:30962433"
FT MOD_RES 803
FT /note="Glycine radical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00493"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 66..80
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 230..260
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 264..279
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 288..305
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 336..352
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 360..364
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 390..401
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 441..450
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 455..459
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 483..485
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 486..494
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 495..497
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 520..549
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 550..552
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 556..560
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 583..589
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 591..604
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 605..607
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 613..621
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 622..626
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 628..634
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 645..665
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 671..677
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 683..688
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 719..727
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 752..768
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 773..778
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 781..789
FT /evidence="ECO:0007829|PDB:5YMR"
FT TURN 791..796
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 798..800
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 802..807
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:5YMR"
FT HELIX 813..821
FT /evidence="ECO:0007829|PDB:5YMR"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:5YMR"
SQ SEQUENCE 828 AA; 93950 MW; D6F4D2E0BE92AF1E CRC64;
MQCCNQLSPH EQRLQDKIEG KVDRYRATHE RVFTILESFD NTRPRIDVER AKYFTESMKA
TEGQPLPLRW AKALMHIAEN MTVYIDDHQL ICGRAGYQGR YGVLYPELDG DFLGTAIEDL
PNRAESPFAI TPEDARVVVE EIAPFWKGKT YHEALNLALP ADVHKLTYDD PQGLMSRFIV
NETSSFRSSI QWVHDYEKVL KRGFRSIKEE ALEKIAALDP MSPCDNVEKR PFLEAIVIVC
DAIILWAKRH AKLAAELAAK ETDPTRKREL ETMAEICAWV PENPARTFHE AVQAQWFTQV
FSRIEQKTGT IVSNGRMDQY FWPFYEKDLA EGRITEDSAL ELLECMWVGM AQYVDLYISP
TGGAFNEGYA HWEAVTIGGQ TPEGRDATND LTYLFLKSKR EFPLHYPDLA ARIHSRSPER
YLWEVAETIK DGSGFPKLIN DEEVVPLYVS KGATFAEALD YAVSGCTEAR MPNRDTYTSG
GAYINFAAAL EMVLYNGKML KYGDTDLGAH TGDPCEFKTW EEFWNAYVTQ HHLFLKTAFV
QQHIINNLRA RHFAQPMGSS LHDLCMKHCL DLHTPQIPEG INLGYFEYMG FGTVVDSLSA
IKKLVFEDKK LTMGELIEAL KCNFEGKEDI QQLLKSAPCY GNNDDYADSI ARDIDALSVK
YGRRYSPELG MHNDVRYVPF TSHVPFGRVV SATPNGRKAW SALSDGSSAS HGADVNGPTA
ILQSNFNSKN YGMRDRAARM LNIKFTPKCV EGEEGSQKLV SFIRTFCDLK LWHVQFNVIN
KETLLAAQRD PEKYRNLIVR IAGYSAYFVD LSPDLQNDLI ARTGHDVM
