DC4C_PSEPU
ID DC4C_PSEPU Reviewed; 48 AA.
AC P00881;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=4-carboxymuconolactone decarboxylase;
DE Short=CMD;
DE EC=4.1.1.44;
DE Flags: Fragment;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7391024; DOI=10.1016/s0021-9258(18)43744-1;
RA Yeh W.-K., Fletcher P., Ornston L.N.;
RT "Homologies in the NH2-terminal amino acid sequences of gamma-
RT carboxymuconolactone decarboxylases and muconolactone isomerases.";
RL J. Biol. Chem. 255:6347-6354(1980).
RN [2]
RP PROTEIN SEQUENCE OF 1-12.
RX PubMed=454663; DOI=10.1016/0005-2795(79)90122-3;
RA Parke D.;
RT "Structural comparison of gamma-carboxymuconolactone decarboxylase and
RT muconolactone isomerase from Pseudomonas putida.";
RL Biochim. Biophys. Acta 578:145-154(1979).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-2-(carboxymethyl)-5-oxo-2,5-dihydro-2-furoate + H(+) =
CC (4,5-dihydro-5-oxofuran-2-yl)-acetate + CO2; Xref=Rhea:RHEA:23348,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58425,
CC ChEBI:CHEBI:58771; EC=4.1.1.44;
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DR PIR; A01101; DCPSMP.
DR AlphaFoldDB; P00881; -.
DR STRING; 1240350.AMZE01000001_gene2845; -.
DR eggNOG; COG0599; Bacteria.
DR BioCyc; MetaCyc:MON-3206; -.
DR GO; GO:0047575; F:4-carboxymuconolactone decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1290.10; -; 1.
DR InterPro; IPR029032; AhpD-like.
DR SUPFAM; SSF69118; SSF69118; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Decarboxylase; Direct protein sequencing;
KW Lyase.
FT CHAIN 1..>48
FT /note="4-carboxymuconolactone decarboxylase"
FT /id="PRO_0000079799"
FT NON_TER 48
SQ SEQUENCE 48 AA; 5570 MW; D1949AD54876B9F1 CRC64;
MDEKQRYDAG MQVRRAVLGD AHVDRCLEKL NDFNGEFQEM ITRHACGD