ID   DLHH_SACS2              Reviewed;         257 AA.
AC   P95862;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Putative carboxymethylenebutenolidase;
DE            EC=3.1.1.45;
DE   AltName: Full=Dienelactone hydrolase;
DE            Short=DLH;
GN   OrderedLocusNames=SSO2087; ORFNames=C06015, C31_045;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x;
RA   Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y.,
RA   Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F.,
RA   Ragan M.A., Charlebois R.L.;
RT   "Organizational characteristics and information content of an archaeal
RT   genome: 156 kb of sequence from Sulfolobus solfataricus P2.";
RL   Mol. Microbiol. 22:175-191(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(5-oxo-2,5-dihydrofuran-2-ylidene)acetate + H2O = 4-oxohex-
CC         2-enedioate + H(+); Xref=Rhea:RHEA:12372, ChEBI:CHEBI:12040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57263; EC=3.1.1.45;
CC   -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC       {ECO:0000305}.
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DR   EMBL; Y08256; CAA69498.1; -; Genomic_DNA.
DR   EMBL; AE006641; AAK42266.1; -; Genomic_DNA.
DR   PIR; S73082; S73082.
DR   RefSeq; WP_009989796.1; NC_002754.1.
DR   AlphaFoldDB; P95862; -.
DR   SMR; P95862; -.
DR   STRING; 273057.SSO2087; -.
DR   ESTHER; sulso-dlhh; Dienelactone_hydrolase.
DR   PRIDE; P95862; -.
DR   EnsemblBacteria; AAK42266; AAK42266; SSO2087.
DR   GeneID; 44130790; -.
DR   KEGG; sso:SSO2087; -.
DR   PATRIC; fig|273057.12.peg.2165; -.
DR   eggNOG; arCOG01659; Archaea.
DR   HOGENOM; CLU_054590_7_2_2; -.
DR   InParanoid; P95862; -.
DR   OMA; PGNDEKG; -.
DR   PhylomeDB; P95862; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0008806; F:carboxymethylenebutenolidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002925; Dienelactn_hydro.
DR   Pfam; PF01738; DLH; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..257
FT                   /note="Putative carboxymethylenebutenolidase"
FT                   /id="PRO_0000161584"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   257 AA;  29016 MW;  B2BD7FACD6126382 CRC64;
     MEKEIFYDSD GAKIRAFLAT PENPKLAVIV IHEIWGLNDN IKDISRRLAN EGYMALAPQL
     YTRNEDVLNE GNIQNVMMKV WSIPPEKRND PNSYQQIMSA LDEKGKKVAE LLVLNRQKTE
     EQMIKDAIKA YEYVSSQGVK KIVSMGFCMG GGLAFQLATE VPLDGTIVFY GRNPQPLEAI
     QKIKGPILGL YAGEDPPIDA GLPDLISAII KYKKDLELKI YPGAYHAFFN DRGRSYNKEA
     AEDAWERVKS FLRRVSK