(data stored in SCRATCH zone)

SWISSPROT: NYLA_PSES8

ID   NYLA_PSES8              Reviewed;         493 AA.
AC   P13397;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=6-aminohexanoate-cyclic-dimer hydrolase;
DE            EC=3.5.2.12;
DE   AltName: Full=Nylon oligomers-degrading enzyme EI;
GN   Name=nylA;
OS   Pseudomonas sp. (strain NK87).
OG   Plasmid.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2722746; DOI=10.1128/jb.171.6.3187-3191.1989;
RA   Tsuchiya K., Fukuyama S., Kanzaki N., Kanagawa K., Negoro S., Okada H.;
RT   "High homology between 6-aminohexanoate-cyclic-dimer hydrolases of
RT   Flavobacterium and Pseudomonas strains.";
RL   J. Bacteriol. 171:3187-3191(1989).
CC   -!- FUNCTION: Catalyzes the hydrolysis of 6-aminohexanoic acid cyclic dimer
CC       (1,8-diazacyclotetradecane-2,9-dione) to form the linear dimer 6-
CC       aminohexanoyl-6-aminohexanoic acid. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-
CC         aminohexanoyl)-6-aminohexanoate; Xref=Rhea:RHEA:16225,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16968, ChEBI:CHEBI:58798; EC=3.5.2.12;
CC   -!- PATHWAY: Xenobiotic degradation; nylon-6 oligomer degradation.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
DR   EMBL; M26952; AAA25908.1; -; Genomic_DNA.
DR   SMR; P13397; -.
DR   PRIDE; P13397; -.
DR   UniPathway; UPA00207; -.
DR   GO; GO:0019874; F:6-aminohexanoate-cyclic-dimer hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0019876; P:nylon catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
DR   PRODOM; P13397.
DR   SWISS-2DPAGE; P13397.
KW   Hydrolase; Nylon degradation; Plasmid.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..493
FT                   /note="6-aminohexanoate-cyclic-dimer hydrolase"
FT                   /id="PRO_0000105251"
FT   ACT_SITE        72
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        174
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   493 AA;  52240 MW;  8043AA7871BBEEE0 CRC64;
     MSKVDLWQDA TAQAELVRSG EISRTELLEA TIAHVQAVNP EINAVIIPLF EKARRESELA
     SGPFAGVPYL LKDLTVVSQG DINTSSIKGM KESGYRADHD AYFVQRMRAA GFVLLGKVNT
     PEMGTQVTTE PEAWGATRNP WNLGRSVGGS SGGSGAAVAA ALSPVAHGND AAGSVRIPAS
     VCGVVGLKPT RGRISPGPLV TDSDNVAGAA HEGLFARSVR DIAALLDVVS GHRPGDTFCA
     PTASRPYAQG ISENPGSLRV GVLTHNPVGD FALDPECAAA ARGAAAALAA LGHDVNDAYP
     EALGDRSFLK DYLTICDVAI AREIERNGEL IGRPLTEDDV EWTSWEMVKR ADQVTGRAFA
     ACVDELRYYA GKVERWWEAG WDLLILPTVT RQTPEIGELM LAKGTDLEGR HTALISGSLR
     MLAFTVPFNV SGQPAISLPI GMSSDGMPIG VQIVAAYGRE DLLLQVAAQL EGALPWVARR
     PQLLNPSRKI PAA
//

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