NYLB_FLASK
ID NYLB_FLASK Reviewed; 392 AA.
AC P07061;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=6-aminohexanoate-dimer hydrolase;
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 PROTEIN SEQUENCE OF 108-115 AND 338-355, AND ACTIVE SITE.
RX PubMed=2512123; DOI=10.1111/j.1432-1033.1989.tb15144.x;
RA Negoro S., Mitamura T., Oka K., Kanagawa K., Okada H.;
RT "Determination of the active-site serine of 6-aminohexanoate-dimer
RT hydrolase.";
RL Eur. J. Biochem. 185:521-524(1989).
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}.
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DR EMBL; X00046; CAA24927.1; -; Genomic_DNA.
DR EMBL; D26094; BAA05087.1; -; Genomic_DNA.
DR PIR; A29516; A29516.
DR PDB; 2E8I; X-ray; 1.45 A; A=1-21.
DR PDB; 2ZLY; X-ray; 1.58 A; A=1-21.
DR PDB; 2ZM0; X-ray; 1.50 A; A=1-21.
DR PDB; 2ZM2; X-ray; 1.55 A; A=1-21.
DR PDB; 2ZM7; X-ray; 1.60 A; A=1-21.
DR PDB; 2ZM8; X-ray; 1.55 A; A=1-21.
DR PDB; 2ZM9; X-ray; 1.50 A; A=1-21.
DR PDB; 2ZMA; X-ray; 1.51 A; A=1-21.
DR PDB; 3A65; X-ray; 1.70 A; A=1-21.
DR PDB; 3A66; X-ray; 1.60 A; A=1-21.
DR PDB; 3VWL; X-ray; 1.60 A; A=1-21.
DR PDB; 3VWM; X-ray; 1.60 A; A=1-21.
DR PDB; 3VWN; X-ray; 1.20 A; X=1-21.
DR PDB; 3VWP; X-ray; 1.55 A; A=1-21.
DR PDB; 3VWQ; X-ray; 1.70 A; A=1-21.
DR PDB; 3VWR; X-ray; 1.65 A; A=1-21.
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; P07061; -.
DR SMR; P07061; -.
DR KEGG; ag:BAA05087; -.
DR BioCyc; MetaCyc:MON-5405; -.
DR BRENDA; 3.5.1.46; 460.
DR UniPathway; UPA00207; -.
DR EvolutionaryTrace; P07061; -.
DR GO; GO:0019875; F:6-aminohexanoate-dimer hydrolase activity; IDA:CACAO.
DR GO; GO:0019876; P:nylon catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 2.
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; Direct protein sequencing; Hydrolase; Nylon degradation;
KW Plasmid.
FT CHAIN 1..392
FT /note="6-aminohexanoate-dimer hydrolase"
FT /id="PRO_0000058011"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /evidence="ECO:0000269|PubMed:2512123"
FT TURN 23..27
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:3VWP"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:3VWN"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3VWN"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:3VWN"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:3VWN"
SQ 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
