NYLC_AGRS5
ID NYLC_AGRS5 Reviewed; 355 AA.
AC Q1EPR5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=6-aminohexanoate-oligomer endohydrolase {ECO:0000305};
DE EC=3.5.1.117 {ECO:0000269|PubMed:17827307};
DE AltName: Full=6-aminohexanoate oligomer hydrolase {ECO:0000303|PubMed:17827307};
DE AltName: Full=Ahx endo-type-oligomer hydrolase {ECO:0000303|PubMed:17827307};
DE AltName: Full=Nylon hydrolase {ECO:0000303|PubMed:22187439};
DE AltName: Full=Nylon-oligomer hydrolase {ECO:0000303|PubMed:21821888};
DE AltName: Full=Nylonase {ECO:0000303|PubMed:22187439};
DE Contains:
DE RecName: Full=6-aminohexanoate-oligomer endohydrolase alpha subunit {ECO:0000305};
DE Contains:
DE RecName: Full=6-aminohexanoate-oligomer endohydrolase beta subunit {ECO:0000305};
GN Name=nylC {ECO:0000303|PubMed:17827307};
OS Agromyces sp. (strain KY5R).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agromyces;
OC unclassified Agromyces.
OX NCBI_TaxID=388924;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 267-276, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND PROTEOLYTIC
RP PROCESSING.
RC STRAIN=KY5R;
RX PubMed=17827307; DOI=10.1128/aem.00777-07;
RA Yasuhira K., Tanaka Y., Shibata H., Kawashima Y., Ohara A., Kato D.,
RA Takeo M., Negoro S.;
RT "6-Aminohexanoate oligomer hydrolases from the alkalophilic bacteria
RT Agromyces sp. strain KY5R and Kocuria sp. strain KY2.";
RL Appl. Environ. Microbiol. 73:7099-7102(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KY5R;
RX PubMed=18215642; DOI=10.1263/jbb.104.521;
RA Yasuhira K., Uedo Y., Takeo M., Kato D., Negoro S.;
RT "Genetic organization of nylon-oligomer-degrading enzymes from alkalophilic
RT bacterium, Agromyces sp. KY5R.";
RL J. Biosci. Bioeng. 104:521-524(2007).
RN [3]
RP CRYSTALLIZATION.
RC STRAIN=KY5R;
RX PubMed=21821888; DOI=10.1107/s1744309111022858;
RA Yasuhira K., Shibata N., Tanaka Y., Kumagai N., Tanaka Y., Nagai K.,
RA Kato D., Takeo M., Negoro S., Higuchi Y.;
RT "Crystallization and X-ray diffraction analysis of nylon-oligomer hydrolase
RT (NylC) from Agromyces sp. KY5R.";
RL Acta Crystallogr. F 67:892-895(2011).
RN [4] {ECO:0007744|PDB:3AXG}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), SUBUNIT, PROTEOLYTIC PROCESSING,
RP AND ACTIVE SITE.
RC STRAIN=KY5R;
RX PubMed=22187439; DOI=10.1074/jbc.m111.321992;
RA Negoro S., Shibata N., Tanaka Y., Yasuhira K., Shibata H., Hashimoto H.,
RA Lee Y.H., Oshima S., Santa R., Oshima S., Mochiji K., Goto Y., Ikegami T.,
RA Nagai K., Kato D., Takeo M., Higuchi Y.;
RT "Three-dimensional structure of nylon hydrolase and mechanism of nylon-6
RT hydrolysis.";
RL J. Biol. Chem. 287:5079-5090(2012).
CC -!- FUNCTION: Involved in the degradation of nylon-6 oligomers. Degrades
CC cyclic and linear oligomers of 6-aminohexanoate (Ahx) with a degree of
CC polymerization greater than three by an endo-type mode. Cannot use Ahx
CC cyclic dimer or the Ahx linear dimer. {ECO:0000269|PubMed:17827307}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-
CC (6-aminohexanoyl)]x.; EC=3.5.1.117;
CC Evidence={ECO:0000269|PubMed:17827307};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.49 mg/ml for Ahx cyclic-oligomer {ECO:0000269|PubMed:17827307};
CC Note=kcat is 11.1 sec(-1) with Ahx cyclic-oligomer as substrate.
CC {ECO:0000269|PubMed:17827307};
CC pH dependence:
CC Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:17827307};
CC -!- PATHWAY: Xenobiotic degradation; nylon-6 oligomer degradation.
CC {ECO:0000269|PubMed:17827307}.
CC -!- SUBUNIT: Heterotetramer composed of 4 alpha/beta heterodimers.
CC {ECO:0000269|PubMed:22187439}.
CC -!- PTM: Expressed as an inactive precursor that is cleaved
CC autocatalytically at Asn266/Thr267 to generate an active enzyme
CC composed of an alpha subunit and a beta subunit.
CC {ECO:0000269|PubMed:17827307, ECO:0000269|PubMed:22187439}.
CC -!- SIMILARITY: Belongs to the peptidase S58 family. {ECO:0000305}.
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DR EMBL; AB262079; BAE95769.2; -; Genomic_DNA.
DR EMBL; AB264778; BAE97622.2; -; Genomic_DNA.
DR PDB; 3AXG; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-355.
DR PDBsum; 3AXG; -.
DR AlphaFoldDB; Q1EPR5; -.
DR SMR; Q1EPR5; -.
DR BRENDA; 3.5.1.117; 10250.
DR UniPathway; UPA00207; -.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0019876; P:nylon catabolic process; IDA:UniProtKB.
DR InterPro; IPR016117; ArgJ-like_dom_sf.
DR InterPro; IPR005321; Peptidase_S58_DmpA.
DR PANTHER; PTHR36512; PTHR36512; 1.
DR Pfam; PF03576; Peptidase_S58; 1.
DR SUPFAM; SSF56266; SSF56266; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hydrolase; Nylon degradation.
FT CHAIN 1..266
FT /note="6-aminohexanoate-oligomer endohydrolase alpha
FT subunit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000452351"
FT CHAIN 267..355
FT /note="6-aminohexanoate-oligomer endohydrolase beta
FT subunit"
FT /evidence="ECO:0000305"
FT /id="PRO_0000452352"
FT ACT_SITE 267
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:22187439"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3AXG"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 70..87
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:3AXG"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 159..167
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 210..218
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 221..225
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:3AXG"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:3AXG"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:3AXG"
FT STRAND 309..318
FT /evidence="ECO:0007829|PDB:3AXG"
FT HELIX 335..354
FT /evidence="ECO:0007829|PDB:3AXG"
SQ SEQUENCE 355 AA; 36891 MW; B5B3547BE21F1A74 CRC64;
MNTTPVHALT DIDGGIAVDP APRLAGPPVF GGPGNDAFDL APVRSTGREM LRFDFPGVSI
GAAHYEEGPT GATVIHIPAG ARTAVDARGG AVGLSGGYDF NHAICLAGGA SYGLEAGAGV
SGALLERLEY RTGFAEAQLV SSAVIYDFSA RSTAVYPDKA LGRAALEFAV PGEFPQGRAG
AGMSASAGKV DWDRTEITGQ GAAFRRLGDV RILAVVVPNP VGVIMDRAGT VVRGNYDAQT
GVRRHPVFDY QEAFAEQVPP VTEAGNTTIS AIVTNVRMSP VELNQFAKQV HSSMHRGIQP
FHTDMDGDTL FAVTTDEIDL PTTPGSSRGR LSVNATALGA IASEVMWDAV LEAGK
