NYLB2_FLASK
ID NYLB2_FLASK Reviewed; 392 AA.
AC P07062;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=6-aminohexanoate-dimer hydrolase {ECO:0000303|PubMed:1879421};
DE EC=3.5.1.46 {ECO:0000305|PubMed:6389532};
DE AltName: Full=6-aminohexanoic acid linear oligomer hydrolase {ECO:0000303|PubMed:6646204};
DE AltName: Full=Nylon oligomers-degrading enzyme EII';
GN Name=nylB' {ECO:0000303|PubMed:6646204};
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], FUNCTION, AND PATHWAY.
RC STRAIN=K172;
RX PubMed=6646204; DOI=10.1038/306203a0;
RA Okada H., Negoro S., Kimura H., Nakamura S.;
RT "Evolutionary adaptation of plasmid-encoded enzymes for degrading nylon
RT oligomers.";
RL Nature 306:203-206(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=6389532; DOI=10.1016/s0021-9258(18)89791-5;
RA Negoro S., Nakamura S., Kimura H., Fujiyama K., Zhang Y.Z., Kanzaki N.,
RA Okada H.;
RT "Construction of hybrid genes of 6-aminohexanoic acid-oligomer hydrolase
RT and its analogous enzyme. Estimation of the intramolecular regions
RT important for the enzyme evolution.";
RL J. Biol. Chem. 259:13648-13651(1984).
RN [3]
RP MUTAGENESIS.
RX PubMed=1879421; DOI=10.1111/j.1432-1033.1991.tb21063.x;
RA Kato K., Fujiyama K., Hatanaka H.S., Priyambada I.D., Negoro S., Urabe I.,
RA Okada H.;
RT "Amino acid alterations essential for increasing the catalytic activity of
RT the nylon-oligomer-degradation enzyme of Flavobacterium sp.";
RL Eur. J. Biochem. 200:165-169(1991).
CC -!- FUNCTION: Involved in nylon oligomer degradation.
CC {ECO:0000269|PubMed:6389532, ECO:0000269|PubMed:6646204}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[N-(6-aminohexanoyl)](n) + H2O = 6-aminohexanoate + [N-(6-
CC aminohexanoyl)](n-1); Xref=Rhea:RHEA:18225, Rhea:RHEA-COMP:9820,
CC Rhea:RHEA-COMP:14302, ChEBI:CHEBI:15377, ChEBI:CHEBI:57826,
CC ChEBI:CHEBI:78629; EC=3.5.1.46;
CC Evidence={ECO:0000305|PubMed:6389532};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(6-aminohexanoyl)-6-aminohexanoate = 2 6-
CC aminohexanoate; Xref=Rhea:RHEA:21364, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57826, ChEBI:CHEBI:58798; EC=3.5.1.46;
CC Evidence={ECO:0000305|PubMed:6389532};
CC -!- PATHWAY: Xenobiotic degradation; nylon-6 oligomer degradation.
CC {ECO:0000305|PubMed:6646204}.
CC -!- MISCELLANEOUS: The EII enzyme is 100 times more active toward the
CC substrate than the EII' enzyme. {ECO:0000269|PubMed:6646204}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X02864; CAA26616.1; -; Genomic_DNA.
DR PDB; 1WYB; X-ray; 1.80 A; A=6-392.
DR PDB; 1WYC; X-ray; 1.58 A; A=9-392.
DR PDB; 2DCF; X-ray; 1.40 A; A=9-392.
DR PDB; 2E8I; X-ray; 1.45 A; A=22-392.
DR PDB; 2ZLY; X-ray; 1.58 A; A=22-392.
DR PDB; 2ZM0; X-ray; 1.50 A; A=22-392.
DR PDB; 2ZM2; X-ray; 1.55 A; A=22-392.
DR PDB; 2ZM7; X-ray; 1.60 A; A=22-392.
DR PDB; 2ZM8; X-ray; 1.55 A; A=22-392.
DR PDB; 2ZM9; X-ray; 1.50 A; A=22-392.
DR PDB; 2ZMA; X-ray; 1.51 A; A=22-392.
DR PDB; 3A65; X-ray; 1.70 A; A=22-392.
DR PDB; 3A66; X-ray; 1.60 A; A=22-392.
DR PDB; 3VWL; X-ray; 1.60 A; A=22-392.
DR PDB; 3VWM; X-ray; 1.60 A; A=22-392.
DR PDB; 3VWN; X-ray; 1.20 A; X=22-392.
DR PDB; 3VWP; X-ray; 1.55 A; A=22-392.
DR PDB; 3VWQ; X-ray; 1.70 A; A=22-392.
DR PDB; 3VWR; X-ray; 1.65 A; A=22-392.
DR PDBsum; 1WYB; -.
DR PDBsum; 1WYC; -.
DR PDBsum; 2DCF; -.
DR PDBsum; 2E8I; -.
DR PDBsum; 2ZLY; -.
DR PDBsum; 2ZM0; -.
DR PDBsum; 2ZM2; -.
DR PDBsum; 2ZM7; -.
DR PDBsum; 2ZM8; -.
DR PDBsum; 2ZM9; -.
DR PDBsum; 2ZMA; -.
DR PDBsum; 3A65; -.
DR PDBsum; 3A66; -.
DR PDBsum; 3VWL; -.
DR PDBsum; 3VWM; -.
DR PDBsum; 3VWN; -.
DR PDBsum; 3VWP; -.
DR PDBsum; 3VWQ; -.
DR PDBsum; 3VWR; -.
DR AlphaFoldDB; P07062; -.
DR SMR; P07062; -.
DR BRENDA; 3.5.1.117; 460.
DR BRENDA; 3.5.1.46; 2302.
DR UniPathway; UPA00207; -.
DR EvolutionaryTrace; P07062; -.
DR GO; GO:0019875; F:6-aminohexanoate-dimer hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0019876; P:nylon catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Nylon degradation; Plasmid.
FT CHAIN 1..392
FT /note="6-aminohexanoate-dimer hydrolase"
FT /id="PRO_0000058012"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /evidence="ECO:0000250|UniProtKB:P07061"
FT MUTAGEN 181
FT /note="G->D: Enhances activity."
FT /evidence="ECO:0000269|PubMed:1879421"
FT MUTAGEN 266
FT /note="H->N: Enhances activity."
FT /evidence="ECO:0000269|PubMed:1879421"
FT TURN 23..27
FT /evidence="ECO:0007829|PDB:2DCF"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:2DCF"
FT STRAND 210..212
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:3VWN"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:2DCF"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2DCF"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:2DCF"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:2DCF"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:3VWN"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 372..388
FT /evidence="ECO:0007829|PDB:3VWN"
SQ SEQUENCE 392 AA; 42647 MW; 527E585107B35EA2 CRC64;
MNTPTTGSHP ARYPSAAAGE PTLDSWQEPP HNRWAFAHLG EMVPSAAVSR RPVNAPGHAL
ARLGAIAAQL PDLEQRLEQT YTDAFLVLRG TEVVAEYYRA GFAPDDRHLL MSVSKSLCGT
VVGALVDEGR IDPAQPVTEY VPELAGSVYD GPSVLQVLDM QISIDYNEDY VDPASEVQTH
GRSAGWRTRA TGDPADTYEF LTTLRGDGST GEFQYCSANT DVLAWIVERV TGLRYVEALS
TYLWAKLDAD RDATITVDTT GFGFAHGGVS CTARDLARVG RMMLDGGVAP GGRVVSEDWV
RRVLAGGSHE AMTDKGFTNT FPDGSYTRQW WCTGNERGNV SGIGIHGQNL WLDPLTDSVI
VKLSSWPDPD TEHWHRLQNG ILLDVSRALD AV
