NYLA_FLASK
ID NYLA_FLASK Reviewed; 493 AA.
AC P13398;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
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 Flavobacterium sp. (strain K172).
OG Plasmid pOAD2.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=37931;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-12.
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).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RX PubMed=923591; DOI=10.1111/j.1432-1033.1977.tb11904.x;
RA Kinoshita S., Negoro S., Muramatsu M., Bisaria V.S., Sawada S., Okada H.;
RT "6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide hydrolase
RT produced by Achromobacter guttatus KI72.";
RL Eur. J. Biochem. 80:489-495(1977).
CC -!- FUNCTION: Specifically catalyzes the hydrolysis of 6-aminohexanoic acid
CC cyclic dimer (1,8-diazacyclotetradecane-2,9-dione) to form the linear
CC dimer 6-aminohexanoyl-6-aminohexanoic acid. Is inactive on 6-
CC aminohexanoic acid oligomers (degree of polymerization 2 to 6), various
CC other cyclic amides, cyclic diamides, linear amides, oligopeptides, and
CC casein. Allows the bacterium to grow on a medium containing 6-
CC aminohexanoic acid cyclic dimer as the sole carbon and nitrogen
CC sources. {ECO:0000269|PubMed:923591}.
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 Evidence={ECO:0000269|PubMed:923591};
CC -!- ACTIVITY REGULATION: Strongly inhibited by 1 uM
CC diisopropylphosphofluoridate and 10 uM p-chloromercuribenzoate but
CC scarcely inhibited by 100 mM EDTA in vitro.
CC {ECO:0000269|PubMed:923591}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6 mM for 1,8-diazacyclotetradecane-2,9-dione
CC {ECO:0000269|PubMed:923591};
CC pH dependence:
CC Optimum pH is 7.3. Is stable from pH 5.5 to 8.5.
CC {ECO:0000269|PubMed:923591};
CC Temperature dependence:
CC Optimum temperature is 33 degrees Celsius. Loses 50% and 100% of
CC activity after 10 minutes of heating at 45 degrees Celsius and 50
CC degrees Celsius, respectively. {ECO:0000269|PubMed:923591};
CC -!- PATHWAY: Xenobiotic degradation; nylon-6 oligomer degradation.
CC {ECO:0000269|PubMed:923591}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:923591}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR EMBL; D26094; BAA05090.1; -; Genomic_DNA.
DR EMBL; M26953; AAA24929.1; -; Genomic_DNA.
DR RefSeq; WP_012476897.1; NZ_BDMH01000055.1.
DR PDB; 3A2P; X-ray; 1.90 A; A=1-493.
DR PDB; 3A2Q; X-ray; 1.80 A; A=1-493.
DR PDBsum; 3A2P; -.
DR PDBsum; 3A2Q; -.
DR AlphaFoldDB; P13398; -.
DR SMR; P13398; -.
DR KEGG; ag:BAA05090; -.
DR BioCyc; MetaCyc:MON-5403; -.
DR UniPathway; UPA00207; -.
DR EvolutionaryTrace; P13398; -.
DR GO; GO:0019874; F:6-aminohexanoate-cyclic-dimer hydrolase activity; IEA:UniProtKB-EC.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Nylon degradation;
KW Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2722746"
FT CHAIN 2..493
FT /note="6-aminohexanoate-cyclic-dimer hydrolase"
FT /id="PRO_0000105252"
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"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 24..42
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:3A2Q"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3A2Q"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 275..290
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 308..331
FT /evidence="ECO:0007829|PDB:3A2Q"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 356..378
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:3A2Q"
FT TURN 396..399
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 416..422
FT /evidence="ECO:0007829|PDB:3A2Q"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 435..442
FT /evidence="ECO:0007829|PDB:3A2Q"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 460..473
FT /evidence="ECO:0007829|PDB:3A2Q"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3A2Q"
SQ SEQUENCE 493 AA; 52212 MW; AAF36B8B30B0FE00 CRC64;
MSKVDLWQDA TAQAELVRSG EISRTELLEA TIAHVQAVNP EINAVIIPLF EKARRESELA
SGPFAGVPYL LKDLTVVSQG DINTSSIKGM KESGYRADHD AYFVQRMRAA GFVLLGKTNT
PEMGNQVTTE PEAWGATRNP WNLGRSVGGS SGGSGAAVAA ALSPVAHGND AAGSVRIPAS
VCGVVGLKPT RGRISPGPLV TDSDNVAGAA HEGLFARSVR DIAALLDVVS GHRPGDTFCA
PTASRPYAQG ISENPGSLRV GVLTHNPVGD FALDPECAAA ARGAAAALAA LGHDVNDAYP
EALGDRSFLK DYSTICDVAI AREIERNGEL IGRPLTEDDV EWTSWEMVKR ADQVTGRAFA
ACVDELRYYA GKVERWWEAG WDLLILPTVT RQTPEIGELM LAKGTDLEGR QSAFISGSLQ
MLAFTVPFNV SGQPAISLPI GMSSDGMPIG VQIVAAYGRE DLLLQVAAQL EGALPWVARR
PQLLNPSRKI PAA
