SLMH_HYDIT
ID SLMH_HYDIT Reviewed; 303 AA.
AC A6XIG6;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=4-sulfomuconolactone hydrolase;
DE EC=3.1.1.92;
DE AltName: Full=4-carboxymethylen-4-sulfo-but-2-en-olide hydrolases;
OS Hydrogenophaga intermedia.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=65786;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, COFACTOR, AND SUBUNIT.
RC STRAIN=DSM 5680 / S1;
RX PubMed=17660282; DOI=10.1128/jb.00611-07;
RA Halak S., Basta T., Burger S., Contzen M., Wray V., Pieper D.H., Stolz A.;
RT "4-sulfomuconolactone hydrolases from Hydrogenophaga intermedia S1 and
RT Agrobacterium radiobacter S2.";
RL J. Bacteriol. 189:6998-7006(2007).
CC -!- FUNCTION: Involved in the degradation of 4-sulfocatechol which is a
CC central intermediate in the degradation of substituted sulfonated
CC benzenes. Catalyzes the hydrolytical desulfonation of 4-
CC sulfomuconolactone to yield maleylacetate.
CC {ECO:0000269|PubMed:17660282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-sulfomuconolactone + H2O = 2 H(+) + maleylacetate + sulfite;
CC Xref=Rhea:RHEA:33711, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16468, ChEBI:CHEBI:17359, ChEBI:CHEBI:20479; EC=3.1.1.92;
CC Evidence={ECO:0000269|PubMed:17660282};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:17660282};
CC -!- ACTIVITY REGULATION: Completely inhibited by ZnCl(2) and CuCl(2).
CC {ECO:0000269|PubMed:17660282}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 mM for 4-sulfomuconolactone (at pH 8)
CC {ECO:0000269|PubMed:17660282};
CC Vmax=79 umol/min/mg enzyme (at pH 8) {ECO:0000269|PubMed:17660282};
CC Note=kcat is 2700 min(-1) with 4-sulfomuconolactone (at pH 8).;
CC pH dependence:
CC Optimum pH is between 7 and 7.5. Approximately 30% of the maximal
CC activities are still detected at pH 5 and pH 9.
CC {ECO:0000269|PubMed:17660282};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17660282}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Sulfomuconolactone hydrolase family. {ECO:0000305}.
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DR EMBL; DQ813261; ABH09754.1; -; Genomic_DNA.
DR AlphaFoldDB; A6XIG6; -.
DR SMR; A6XIG6; -.
DR KEGG; ag:ABH09754; -.
DR BioCyc; MetaCyc:MON-14206; -.
DR BRENDA; 3.1.1.92; 9756.
DR GO; GO:0102998; F:4-sulfomuconolactone hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0018732; F:sulfolactone hydrolase activity; IEA:UniProtKB-EC.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW Hydrolase.
FT CHAIN 1..303
FT /note="4-sulfomuconolactone hydrolase"
FT /id="PRO_0000422786"
SQ SEQUENCE 303 AA; 34092 MW; A10170BB58D839D9 CRC64;
MSEQAVEVSP KCLGPQHHIN PLRFVMPPGS WDTHFHVFGP TTKYPYSETR KYTPPDSPFE
EYVKLMLALG IERGVCVHPN IHGPDNSVTL DAVERSEGRF LAIVKIAPDV TLPQLKEMKK
KGACGVRFAF NPEHGSGELD TALFDRVVQW CGELDWCVNL HFASNAIHSL AERLSQLTIP
TLIDHFGRVH PTKGVDQPDF KTLVDLMRLP HMWVKLTGAD RISRNSPSYQ DVVPLARTLV
DVAPDRVIWG TDWPHSGYFD VKRMPNDGDL TNLLLDFAPS EEQRRRILVD NPSRLFGQVA
KGA