ISLB_DESVH
ID ISLB_DESVH Reviewed; 307 AA.
AC Q727N0;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Isethionate sulfite-lyase activating enzyme;
DE EC=1.97.1.- {ECO:0000305|PubMed:30962433};
DE AltName: Full=GRE activase IseH;
DE AltName: Full=Glycyl-radical enzyme activating enzyme IseH;
GN Name=iseH {ECO:0000303|PubMed:30962433};
GN OrderedLocusNames=DVU_2825 {ECO:0000312|EMBL:AAS97297.1};
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]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
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 activation of the isethionate sulfite-
CC lyase IseG under anaerobic conditions by generation of an organic free
CC radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-
CC methionine (SAM). {ECO:0000269|PubMed:30962433}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-
CC methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+)
CC + L-methionine + semiquinone [flavodoxin]; Xref=Rhea:RHEA:61976,
CC Rhea:RHEA-COMP:10622, Rhea:RHEA-COMP:14480, Rhea:RHEA-COMP:15993,
CC Rhea:RHEA-COMP:15994, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319,
CC ChEBI:CHEBI:29947, ChEBI:CHEBI:32722, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:140311;
CC Evidence={ECO:0000305|PubMed:30962433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61977;
CC Evidence={ECO:0000305|PubMed:30962433};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711,
CC ECO:0000269|PubMed:30962433};
CC Note=Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000305|PubMed:30962433}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q30W71}.
CC -!- INTERACTION:
CC Q727N0; Q728C6: DVU_2677; NbExp=2; IntAct=EBI-10066541, EBI-10066547;
CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes family.
CC {ECO:0000305}.
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DR EMBL; AE017285; AAS97297.1; -; Genomic_DNA.
DR RefSeq; WP_010940091.1; NC_002937.3.
DR RefSeq; YP_012037.1; NC_002937.3.
DR AlphaFoldDB; Q727N0; -.
DR SMR; Q727N0; -.
DR IntAct; Q727N0; 1.
DR STRING; 882.DVU_2825; -.
DR PaxDb; Q727N0; -.
DR EnsemblBacteria; AAS97297; AAS97297; DVU_2825.
DR KEGG; dvu:DVU_2825; -.
DR PATRIC; fig|882.5.peg.2553; -.
DR eggNOG; COG1180; Bacteria.
DR HOGENOM; CLU_058969_0_0_7; -.
DR OMA; PWKYIEP; -.
DR PhylomeDB; Q727N0; -.
DR UniPathway; UPA00338; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040074; BssD/PflA/YjjW.
DR InterPro; IPR034457; Organic_radical-activating.
DR InterPro; IPR012839; Organic_radical_activase.
DR InterPro; IPR001989; Radical_activat_CS.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR30352; PTHR30352; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR PIRSF; PIRSF000371; PFL_act_enz; 1.
DR SFLD; SFLDG01118; activating_enzymes__group_2; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS01087; RADICAL_ACTIVATING; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase;
KW Reference proteome; Repeat; S-adenosyl-L-methionine.
FT CHAIN 1..307
FT /note="Isethionate sulfite-lyase activating enzyme"
FT /id="PRO_0000450948"
FT DOMAIN 22..307
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT DOMAIN 53..85
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 86..117
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 36
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 40
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 42..44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 71
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 75
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 95
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 102
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 146
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 195..197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
FT BINDING 268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P0A9N4"
SQ SEQUENCE 307 AA; 33738 MW; 017AA3D4880B0695 CRC64;
MSSIADRKTT GITFNIQKYS VHDGPGIRTV VFLKGCPLKC RWCSNPESQR KSVELAYNTG
RCLTLAKCVR CVEICTAGAI SRAEDDTISI DRALCNDCEQ LCSGACPSNA LITYGAHKTV
DEVLRAVEQD SLFYARSGGG MTISGGEPFA QPAFTLALLR EARRRRVHTA VETCGYASWD
DMAAALPFLN YVLYDIKNLD DARHKEATGV SNQRIVENLR ALRAEFPGIP VLVRTPVIPG
FNDNEADIAA IAALTRELGV SYQLLPYHRL GTQKYHFLDR EAPMGEVTLD AETMRRLEAV
VAQTADS
