ID A0A244EJE9_9BURK Unreviewed; 227 AA.
AC A0A244EJE9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE RecName: Full=carboxymethylenebutenolidase {ECO:0000256|ARBA:ARBA00044062};
DE EC=3.1.1.45 {ECO:0000256|ARBA:ARBA00044062};
GN ORFNames=A8M77_00130 {ECO:0000313|EMBL:OUM04164.1};
OS Variovorax sp. JS1663.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM04164.1, ECO:0000313|Proteomes:UP000195166};
RN [1] {ECO:0000313|EMBL:OUM04164.1, ECO:0000313|Proteomes:UP000195166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1663 {ECO:0000313|EMBL:OUM04164.1};
RX PubMed=28526789;
RA Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL Appl. Environ. Microbiol. 83:0-0(2017).
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:OUM04164.1}.
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DR EMBL; LYMK01000001; OUM04164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A244EJE9; -.
DR OrthoDB; 62567at2; -.
DR Proteomes; UP000195166; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002925; Dienelactn_hydro.
DR PANTHER; PTHR46623; CARBOXYMETHYLENEBUTENOLIDASE-RELATED; 1.
DR PANTHER; PTHR46623:SF11; CARBOXYMETHYLENEBUTENOLIDASE-RELATED; 1.
DR Pfam; PF01738; DLH; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000195166}.
FT DOMAIN 15..225
FT /note="Dienelactone hydrolase"
FT /evidence="ECO:0000259|Pfam:PF01738"
SQ SEQUENCE 227 AA; 24065 MW; 81B0D1994D150A4B CRC64;
MGQFIDLTAK DGVAFPAYVA EPAGKPKGAV VVVQEIFGVN SHIRSVADGY AAEGYLAVAP
ATFHRVKPGV ELGYSEDDMK AGFSLKTAVE ALPAPGVLQD LQAAVDYAAR AGKVGIVGYC
WGGLLTWRAS AKVSGLSAAA PYYGGGMTTP EESAITPKVP VLAHFGNNDH WIPLDTIETF
KKAHPEVEVH VYECGHGFNC DQRGSYNAEA AKLARERTLA FFAKHLA
//