ID   AMNE_PSESP              Reviewed;         256 AA.
AC   Q9KWS3;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=4-oxalocrotonate decarboxylase;
DE            EC=4.1.1.77;
GN   Name=amnE;
OS   Pseudomonas sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AP-3;
RX   PubMed=9169437; DOI=10.1074/jbc.272.23.14727;
RA   Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K.;
RT   "Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas
RT   species AP-3 growing on 2-aminophenol and catalytic properties of the
RT   purified enzyme.";
RL   J. Biol. Chem. 272:14727-14732(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND ACTIVITY REGULATION.
RC   STRAIN=AP-3;
RX   PubMed=11081795; DOI=10.1007/s002030000203;
RA   Takenaka S., Murakami S., Kim Y.J., Aoki K.;
RT   "Complete nucleotide sequence and functional analysis of the genes for 2-
RT   aminophenol metabolism from Pseudomonas sp. AP-3.";
RL   Arch. Microbiol. 174:265-272(2000).
CC   -!- FUNCTION: Involved in the modified meta-cleavage pathway for the 2-
CC       aminophenol catabolism. {ECO:0000269|PubMed:9169437}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3E)-2-oxohex-3-enedioate + H(+) = 2-oxopent-4-enoate + CO2;
CC         Xref=Rhea:RHEA:24260, ChEBI:CHEBI:11641, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:64908; EC=4.1.1.77;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:11081795};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:11081795};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Fe(2+), Fe(3+),
CC       K(3)[Fe(CN)(6)], Ag(+) and Cu(2+). {ECO:0000269|PubMed:11081795}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. Stable in the range of pH 5.0-8.0.
CC         {ECO:0000269|PubMed:11081795};
CC       Temperature dependence:
CC         Stable up to 35 degrees Celsius. {ECO:0000269|PubMed:11081795};
CC   -!- SUBUNIT: Forms a complex with AmnF. {ECO:0000269|PubMed:11081795}.
CC   -!- SIMILARITY: Belongs to the hydratase/decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; AB020521; BAB03535.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9KWS3; -.
DR   SMR; Q9KWS3; -.
DR   BioCyc; MetaCyc:MON-14743; -.
DR   GO; GO:0047437; F:4-oxalocrotonate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Direct protein sequencing; Lyase;
KW   Magnesium; Manganese.
FT   CHAIN           1..256
FT                   /note="4-oxalocrotonate decarboxylase"
FT                   /id="PRO_0000383024"
SQ   SEQUENCE   256 AA;  27196 MW;  F9C4323D72434F82 CRC64;
     MKISRIAQRL DEAAVSGKAT PQLTGDDAVT VREAAEIQRL LIAHRIERGA RQVGLKMGFT
     SRAKMAQMGV SDLIWGRLTS DMWVEEGGEI DLAHYVHPRV EPEICYLLGK RLEGNVTPLE
     ALAAVEAVAP AMEIIDSRYR DFKFSLPDVI ADNASSSGFV VGAWHKPETD VSNLGMVMSF
     DGRAVELGTS AAILGSPIRA LVAAARLAAQ QGEALEAGSL ILAGAATAAV ALRPGISVRC
     EVQNLGSLSF STTGER