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6-aminohexanoate-dimer hydrolase (EC 3.5.1.46) (Nylon oligomers-degrading enzyme EII)

 NYLB_FLASK              Reviewed;         392 AA.
P07061;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
10-MAY-2017, entry version 81.
RecName: Full=6-aminohexanoate-dimer hydrolase;
EC=3.5.1.46;
AltName: Full=Nylon oligomers-degrading enzyme EII;
Name=nylB;
Flavobacterium sp. (strain K172).
Plasmid pOAD2.
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Flavobacterium.
NCBI_TaxID=261;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6646204; DOI=10.1038/306203a0;
Okada H., Negoro S., Kimura H., Nakamura S.;
"Evolutionary adaptation of plasmid-encoded enzymes for degrading
nylon oligomers.";
Nature 306:203-206(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6389532;
Negoro S., Nakamura S., Kimura H., Fujiyama K., Zhang Y.Z.,
Kanzaki N., Okada H.;
"Construction of hybrid genes of 6-aminohexanoic acid-oligomer
hydrolase and its analogous enzyme. Estimation of the intramolecular
regions important for the enzyme evolution.";
J. Biol. Chem. 259:13648-13651(1984).
[3]
ACTIVE SITE.
PubMed=2512123; DOI=10.1111/j.1432-1033.1989.tb15144.x;
Negoro S., Mitamura T., Oka K., Kanagawa K., Okada H.;
"Determination of the active-site serine of 6-aminohexanoate-dimer
hydrolase.";
Eur. J. Biochem. 185:521-524(1989).
-!- CATALYTIC ACTIVITY: (N-(6-aminohexanoyl))(n) + H(2)O = (N-(6-
aminohexanoyl))(n-1) + 6-aminohexanoate.
-!- CATALYTIC ACTIVITY: N-(6-aminohexanoyl)-6-aminohexanoate + H(2)O =
2 6-aminohexanoate.
-!- PATHWAY: Xenobiotic degradation; nylon-6 oligomer degradation.
-!- MISCELLANEOUS: The EII enzyme is 100 times more active toward the
substrate than the EII' enzyme.
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EMBL; X00046; CAA24927.1; -; Genomic_DNA.
EMBL; D26094; BAA05087.1; -; Genomic_DNA.
PIR; A29516; A29516.
PDB; 2E8I; X-ray; 1.45 A; A=1-21.
PDB; 2ZLY; X-ray; 1.58 A; A=1-21.
PDB; 2ZM0; X-ray; 1.50 A; A=1-21.
PDB; 2ZM2; X-ray; 1.55 A; A=1-21.
PDB; 2ZM7; X-ray; 1.60 A; A=1-21.
PDB; 2ZM8; X-ray; 1.55 A; A=1-21.
PDB; 2ZM9; X-ray; 1.50 A; A=1-21.
PDB; 2ZMA; X-ray; 1.51 A; A=1-21.
PDB; 3A65; X-ray; 1.70 A; A=1-21.
PDB; 3A66; X-ray; 1.60 A; A=1-21.
PDB; 3VWL; X-ray; 1.60 A; A=1-21.
PDB; 3VWM; X-ray; 1.60 A; A=1-21.
PDB; 3VWN; X-ray; 1.20 A; X=1-21.
PDB; 3VWP; X-ray; 1.55 A; A=1-21.
PDB; 3VWQ; X-ray; 1.70 A; A=1-21.
PDB; 3VWR; X-ray; 1.65 A; A=1-21.
PDBsum; 2E8I; -.
PDBsum; 2ZLY; -.
PDBsum; 2ZM0; -.
PDBsum; 2ZM2; -.
PDBsum; 2ZM7; -.
PDBsum; 2ZM8; -.
PDBsum; 2ZM9; -.
PDBsum; 2ZMA; -.
PDBsum; 3A65; -.
PDBsum; 3A66; -.
PDBsum; 3VWL; -.
PDBsum; 3VWM; -.
PDBsum; 3VWN; -.
PDBsum; 3VWP; -.
PDBsum; 3VWQ; -.
PDBsum; 3VWR; -.
ProteinModelPortal; P07061; -.
SMR; P07061; -.
KEGG; ag:BAA05087; -.
KO; K01453; -.
UniPathway; UPA00207; -.
EvolutionaryTrace; P07061; -.
GO; GO:0019875; F:6-aminohexanoate-dimer hydrolase activity; IDA:CACAO.
GO; GO:0019876; P:nylon catabolic process; IEA:UniProtKB-KW.
InterPro; IPR001466; Beta-lactam-related.
InterPro; IPR012338; Beta-lactam/transpept-like.
Pfam; PF00144; Beta-lactamase; 1.
SUPFAM; SSF56601; SSF56601; 1.
1: Evidence at protein level;
3D-structure; Hydrolase; Nylon degradation; Plasmid.
CHAIN 1 392 6-aminohexanoate-dimer hydrolase.
/FTId=PRO_0000058011.
ACT_SITE 112 112 {ECO:0000269|PubMed:2512123}.
TURN 23 27 {ECO:0000244|PDB:2E8I}.
HELIX 31 35 {ECO:0000244|PDB:2E8I}.
HELIX 39 41 {ECO:0000244|PDB:2E8I}.
STRAND 60 62 {ECO:0000244|PDB:2E8I}.
TURN 67 69 {ECO:0000244|PDB:2E8I}.
SEQUENCE 392 AA; 42693 MW; 9CF34C393C3E53D9 CRC64;
MNARSTGQHP ARYPGAAAGE PTLDSWQEAP HNRWAFARLG ELLPTAAVSR RDPATPAEPV
VRLDALATRL PDLEQRLEET CTDAFLVLRG SEVLAEYYRA GFAPDDRHLL MSVSKSLCGT
VVGALIDEGR IDPAQPVTEY VPELAGSVYD GPSVLQVLDM QISIDYNEDY VDPASEVQTH
DRSAGWRTRR DGDPADTYEF LTTLRGDGGT GEFQYCSANT DVLAWIVERV TGLRYVEALS
TYLWAKLDAD RDATITVDQT GFGFANGGVS CTARDLARVG RMMLDGGVAP GGRVVSQGWV
ESVLAGGSRE AMTDEGFTSA FPEGSYTRQW WCTGNERGNV SGIGIHGQNL WLDPRTDSVI
VKLSSWPDPD TRHWHGLQSG ILLDVSRALD AV


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