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6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12) (Nylon oligomers-degrading enzyme EI)

 NYLA_FLASK              Reviewed;         493 AA.
P13398;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
15-MAR-2017, entry version 80.
RecName: Full=6-aminohexanoate-cyclic-dimer hydrolase;
EC=3.5.2.12;
AltName: Full=Nylon oligomers-degrading enzyme EI;
Name=nylA;
Flavobacterium sp. (strain K172).
Plasmid pOAD2.
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Flavobacterium.
NCBI_TaxID=261;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-12.
PubMed=2722746; DOI=10.1128/jb.171.6.3187-3191.1989;
Tsuchiya K., Fukuyama S., Kanzaki N., Kanagawa K., Negoro S.,
Okada H.;
"High homology between 6-aminohexanoate-cyclic-dimer hydrolases of
Flavobacterium and Pseudomonas strains.";
J. Bacteriol. 171:3187-3191(1989).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, PATHWAY, AND
SUBUNIT.
PubMed=923591; DOI=10.1111/j.1432-1033.1977.tb11904.x;
Kinoshita S., Negoro S., Muramatsu M., Bisaria V.S., Sawada S.,
Okada H.;
"6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide
hydrolase produced by Achromobacter guttatus KI72.";
Eur. J. Biochem. 80:489-495(1977).
-!- FUNCTION: Specifically catalyzes the hydrolysis of 6-aminohexanoic
acid cyclic dimer (1,8-diazacyclotetradecane-2,9-dione) to form
the linear dimer 6-aminohexanoyl-6-aminohexanoic acid. Is inactive
on 6-aminohexanoic acid oligomers (degree of polymerization 2 to
6), various other cyclic amides, cyclic diamides, linear amides,
oligopeptides, and casein. Allows the bacterium to grow on a
medium containing 6-aminohexanoic acid cyclic dimer as the sole
carbon and nitrogen sources. {ECO:0000269|PubMed:923591}.
-!- CATALYTIC ACTIVITY: 1,8-diazacyclotetradecane-2,9-dione + H(2)O =
N-(6-aminohexanoyl)-6-aminohexanoate. {ECO:0000269|PubMed:923591}.
-!- ENZYME REGULATION: Strongly inhibited by 1 uM
diisopropylphosphofluoridate and 10 uM p-chloromercuribenzoate but
scarcely inhibited by 100 mM EDTA in vitro.
{ECO:0000269|PubMed:923591}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6 mM for 1,8-diazacyclotetradecane-2,9-dione
{ECO:0000269|PubMed:923591};
pH dependence:
Optimum pH is 7.3. Is stable from pH 5.5 to 8.5.
{ECO:0000269|PubMed:923591};
Temperature dependence:
Optimum temperature is 33 degrees Celsius. Loses 50% and 100% of
activity after 10 minutes of heating at 45 degrees Celsius and
50 degrees Celsius, respectively. {ECO:0000269|PubMed:923591};
-!- PATHWAY: Xenobiotic degradation; nylon-6 oligomer degradation.
{ECO:0000269|PubMed:923591}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:923591}.
-!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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EMBL; D26094; BAA05090.1; -; Genomic_DNA.
EMBL; M26953; AAA24929.1; -; Genomic_DNA.
PDB; 3A2P; X-ray; 1.90 A; A=1-493.
PDB; 3A2Q; X-ray; 1.80 A; A=1-493.
PDBsum; 3A2P; -.
PDBsum; 3A2Q; -.
ProteinModelPortal; P13398; -.
SMR; P13398; -.
KEGG; ag:BAA05090; -.
KO; K01471; -.
UniPathway; UPA00207; -.
EvolutionaryTrace; P13398; -.
GO; GO:0019874; F:6-aminohexanoate-cyclic-dimer hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004040; F:amidase activity; IEA:InterPro.
GO; GO:0019876; P:nylon catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.90.1300.10; -; 1.
InterPro; IPR000120; Amidase.
InterPro; IPR020556; Amidase_CS.
InterPro; IPR023631; Amidase_dom.
PANTHER; PTHR11895; PTHR11895; 1.
Pfam; PF01425; Amidase; 1.
SUPFAM; SSF75304; SSF75304; 1.
PROSITE; PS00571; AMIDASES; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Hydrolase; Nylon degradation;
Plasmid.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2722746}.
CHAIN 2 493 6-aminohexanoate-cyclic-dimer hydrolase.
/FTId=PRO_0000105252.
ACT_SITE 72 72 Charge relay system. {ECO:0000250}.
ACT_SITE 150 150 Charge relay system. {ECO:0000250}.
ACT_SITE 174 174 Acyl-ester intermediate. {ECO:0000250}.
HELIX 10 19 {ECO:0000244|PDB:3A2Q}.
STRAND 20 22 {ECO:0000244|PDB:3A2Q}.
HELIX 24 42 {ECO:0000244|PDB:3A2Q}.
STRAND 45 48 {ECO:0000244|PDB:3A2Q}.
HELIX 50 59 {ECO:0000244|PDB:3A2Q}.
TURN 63 66 {ECO:0000244|PDB:3A2Q}.
STRAND 68 76 {ECO:0000244|PDB:3A2Q}.
HELIX 88 93 {ECO:0000244|PDB:3A2Q}.
HELIX 102 110 {ECO:0000244|PDB:3A2Q}.
STRAND 113 118 {ECO:0000244|PDB:3A2Q}.
HELIX 122 124 {ECO:0000244|PDB:3A2Q}.
STRAND 126 128 {ECO:0000244|PDB:3A2Q}.
TURN 132 134 {ECO:0000244|PDB:3A2Q}.
STRAND 149 151 {ECO:0000244|PDB:3A2Q}.
HELIX 152 159 {ECO:0000244|PDB:3A2Q}.
STRAND 164 173 {ECO:0000244|PDB:3A2Q}.
HELIX 176 182 {ECO:0000244|PDB:3A2Q}.
STRAND 184 188 {ECO:0000244|PDB:3A2Q}.
HELIX 202 207 {ECO:0000244|PDB:3A2Q}.
STRAND 211 218 {ECO:0000244|PDB:3A2Q}.
HELIX 219 229 {ECO:0000244|PDB:3A2Q}.
HELIX 247 250 {ECO:0000244|PDB:3A2Q}.
STRAND 259 262 {ECO:0000244|PDB:3A2Q}.
HELIX 275 290 {ECO:0000244|PDB:3A2Q}.
STRAND 294 297 {ECO:0000244|PDB:3A2Q}.
HELIX 301 304 {ECO:0000244|PDB:3A2Q}.
HELIX 308 331 {ECO:0000244|PDB:3A2Q}.
TURN 337 339 {ECO:0000244|PDB:3A2Q}.
HELIX 342 352 {ECO:0000244|PDB:3A2Q}.
HELIX 356 378 {ECO:0000244|PDB:3A2Q}.
STRAND 383 388 {ECO:0000244|PDB:3A2Q}.
TURN 396 399 {ECO:0000244|PDB:3A2Q}.
HELIX 412 414 {ECO:0000244|PDB:3A2Q}.
HELIX 416 422 {ECO:0000244|PDB:3A2Q}.
TURN 423 426 {ECO:0000244|PDB:3A2Q}.
HELIX 427 431 {ECO:0000244|PDB:3A2Q}.
STRAND 435 442 {ECO:0000244|PDB:3A2Q}.
STRAND 448 456 {ECO:0000244|PDB:3A2Q}.
HELIX 460 473 {ECO:0000244|PDB:3A2Q}.
HELIX 482 484 {ECO:0000244|PDB:3A2Q}.
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


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