AMND_PSESP
ID AMND_PSESP Reviewed; 142 AA.
AC Q9KWS2;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=2-aminomuconate deaminase;
DE EC=3.5.99.5;
GN Name=amnD;
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, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, SUBUNIT,
RP 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. Only active toward 2-aminomuconic acid.
CC {ECO:0000269|PubMed:9169437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,4E)-2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate +
CC NH4(+); Xref=Rhea:RHEA:20996, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:64908, ChEBI:CHEBI:77859; EC=3.5.99.5;
CC Evidence={ECO:0000269|PubMed:11081795};
CC -!- ACTIVITY REGULATION: Slightly inhibited by Pb(2+), Hg(+) and Cu(2+).
CC {ECO:0000269|PubMed:11081795}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.0. Stable in the range of pH 5.5-8.0.
CC {ECO:0000269|PubMed:11081795};
CC Temperature dependence:
CC Stable up to 55 degrees Celsius. {ECO:0000269|PubMed:11081795};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11081795}.
CC -!- SIMILARITY: Belongs to the 2-aminomuconate deaminase family.
CC {ECO:0000305}.
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DR EMBL; AB020521; BAB03536.1; -; Genomic_DNA.
DR PDB; 6IZH; X-ray; 1.75 A; A/B/C/D/E/F/G/H/I=1-142.
DR PDBsum; 6IZH; -.
DR AlphaFoldDB; Q9KWS2; -.
DR SMR; Q9KWS2; -.
DR KEGG; ag:BAB03536; -.
DR BioCyc; MetaCyc:MON-14742; -.
DR GO; GO:0050540; F:2-aminomuconate deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1330.40; -; 1.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR11803; PTHR11803; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF55298; SSF55298; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW Hydrolase.
FT CHAIN 1..142
FT /note="2-aminomuconate deaminase"
FT /id="PRO_0000383028"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:6IZH"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:6IZH"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:6IZH"
FT HELIX 61..78
FT /evidence="ECO:0007829|PDB:6IZH"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6IZH"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6IZH"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:6IZH"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:6IZH"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:6IZH"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6IZH"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:6IZH"
SQ SEQUENCE 142 AA; 15533 MW; 762ECDEF3B376E36 CRC64;
MVSKADNSAK LVEGKAKPMG SFPHVKRAGD FLFVSGTSSR RPDNTFVGAE PDDTGRPRPN
IELQTREVIS NIRDILQSVG ADLGDVVEVC SYLVNMNDFA AYNKVYAEFF DATGPARTTV
AVHQLPHPQL VIEIKVVAYK PL