SARD_BILW3
ID SARD_BILW3 Reviewed; 387 AA.
AC E5Y946;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Sulfoacetaldehyde reductase {ECO:0000303|PubMed:30718429};
DE EC=1.1.1.- {ECO:0000269|PubMed:30718429, ECO:0000269|PubMed:30962433};
GN Name=sarD {ECO:0000303|PubMed:30718429};
GN Synonyms=tauF {ECO:0000303|PubMed:30962433};
GN ORFNames=HMPREF0179_02714 {ECO:0000312|EMBL:EFV43471.1};
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, INDUCTION BY TAURINE, AND PATHWAY.
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY
RP TAURINE, 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 NADH-dependent reduction of sulfoacetaldehyde to
CC 2-hydroxyethane-1-sulfonate (isethionate). Does not accept acetaldehyde
CC as a substrate. {ECO:0000269|PubMed:30718429,
CC ECO:0000269|PubMed:30962433}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyethane-1-sulfonate + NAD(+) = H(+) + NADH +
CC sulfoacetaldehyde; Xref=Rhea:RHEA:64516, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58246,
CC ChEBI:CHEBI:61904; Evidence={ECO:0000269|PubMed:30718429,
CC ECO:0000269|PubMed:30962433};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64517;
CC Evidence={ECO:0000269|PubMed:30718429, ECO:0000269|PubMed:30962433};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.51 mM for sulfoacetaldehyde {ECO:0000269|PubMed:30718429};
CC Vmax=351 nmol/min/mg enzyme {ECO:0000269|PubMed:30718429};
CC -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC {ECO:0000269|PubMed:30718429, ECO:0000269|PubMed:30962433}.
CC -!- INDUCTION: Up-regulated in the presence of taurine.
CC {ECO:0000269|PubMed:30718429, ECO:0000269|PubMed:30962433}.
CC -!- MISCELLANEOUS: In contrast to some members of the family, a metal
CC cofactor is not required for catalytic activity.
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 iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; ADCP02000001; EFV43471.1; -; Genomic_DNA.
DR RefSeq; WP_005028754.1; NZ_KE150238.1.
DR AlphaFoldDB; E5Y946; -.
DR SMR; E5Y946; -.
DR STRING; 563192.HMPREF0179_02714; -.
DR EnsemblBacteria; EFV43471; EFV43471; HMPREF0179_02714.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_7; -.
DR BioCyc; MetaCyc:MON-20850; -.
DR UniPathway; UPA00338; -.
DR Proteomes; UP000006034; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
DR GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..387
FT /note="Sulfoacetaldehyde reductase"
FT /id="PRO_0000450950"
SQ SEQUENCE 387 AA; 40853 MW; 28C9D19E55E187AB CRC64;
MAFVHYTVKK IVHGLGAIKE AANEVKNLKG SKAFIVTDPG LAKIGVQKPL EEALTAGGIE
WKLYAEAQLE PSMDSIQHCT DEAKAFGADV IIGFGGGSAL DTTKAASVLL SNEGPIDKYF
GINLVPNPSL PCILIPTTSG TGSEMTNISV LADTKNGGKK GVVSEYMYAD TVILDAELTF
GLPPRVTAMT GVDAFVHAME SFCGIAATPI TDALNLQAMK LVGANIRQAY ANGKNAAARD
AMMYASALAG MGFGNTQNGI IHAIGTTLPV ECHIPHGLAM SFCAPFSVGF NYIANPEKYA
IVADILRGDD RSGCMSVMDR AADVEDAFRD LLNDLDIATG LSNYGVKRED LPACADRAFA
AKRLLNNNPR AASRDQILAL LEANFEA
