ID A0A0Q4Y6M4_9BURK Unreviewed; 413 AA.
AC A0A0Q4Y6M4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=carboxymethylenebutenolidase {ECO:0000256|ARBA:ARBA00044062};
DE EC=3.1.1.45 {ECO:0000256|ARBA:ARBA00044062};
GN ORFNames=ASF43_14005 {ECO:0000313|EMBL:KQP15137.1};
OS Pseudorhodoferax sp. Leaf267.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP15137.1, ECO:0000313|Proteomes:UP000051560};
RN [1] {ECO:0000313|EMBL:KQP15137.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP15137.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP15137.1, ECO:0000313|Proteomes:UP000051560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf267 {ECO:0000313|EMBL:KQP15137.1,
RC ECO:0000313|Proteomes:UP000051560};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00043789};
CC -!- SIMILARITY: Belongs to the dienelactone hydrolase family.
CC {ECO:0000256|ARBA:ARBA00008456}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQP15137.1}.
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DR EMBL; LMMV01000021; KQP15137.1; -; Genomic_DNA.
DR RefSeq; WP_056184434.1; NZ_LMMV01000021.1.
DR AlphaFoldDB; A0A0Q4Y6M4; -.
DR STRING; 1736316.ASF43_14005; -.
DR OrthoDB; 62567at2; -.
DR Proteomes; UP000051560; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.10.450.50; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002925; Dienelactn_hydro.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR037401; SnoaL-like.
DR PANTHER; PTHR46623; CARBOXYMETHYLENEBUTENOLIDASE-RELATED; 1.
DR PANTHER; PTHR46623:SF11; CARBOXYMETHYLENEBUTENOLIDASE-RELATED; 1.
DR Pfam; PF01738; DLH; 1.
DR Pfam; PF12680; SnoaL_2; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000051560}.
FT DOMAIN 21..235
FT /note="Dienelactone hydrolase"
FT /evidence="ECO:0000259|Pfam:PF01738"
FT DOMAIN 258..362
FT /note="SnoaL-like"
FT /evidence="ECO:0000259|Pfam:PF12680"
SQ SEQUENCE 413 AA; 44715 MW; 40330059DDF1755B CRC64;
MAHKPSSQYI DIPAADGSGT FRGYLALPSA GTGPGLVIAQ EIFGVNATMR EVADAYAEEG
YVALVPDLFW RQQPGIELGY TPDDWQRAFA LYKGFDEARG VDDIQSAISV LRQRAEVPGR
QVGVLGFCLG GKLAYLAACR TDADVAVGYY GVGIESALDE AAHIQAPLLL HIAEQDGFCP
PEARAQILQA LRGHPKVQAQ VYPGVDHAFA RVGGDHYHRS SALLAHERSI ATLKAAIGPH
YDLAALWDKH CEYEFGLRDV DATMATMVAE PYVNHIPTMT GGVGYEKLHH FYTHHFVNSN
PPDTALVPIS RTVGATQVVD EMLFSFTHTC EIPWMLPGVK PTGKRVEVPL LAVVKFRGDK
LCHEHIYWDQ ASVLVQVGLL DAKLLPVAGV ETARKLVDES LPSNTLMPGG GAA
//
