Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

6-aminohexanoate-dimer hydrolase

Gene

nylB

Organism
Flavobacterium sp. (strain K172)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(N-(6-aminohexanoyl))(n) + H2O = (N-(6-aminohexanoyl))(n-1) + 6-aminohexanoate.
N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate.

Pathwayi: nylon-6 oligomer degradation

This protein is involved in the pathway nylon-6 oligomer degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway nylon-6 oligomer degradation and in Xenobiotic degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei112 – 11211 Publication

GO - Molecular functioni

  • 6-aminohexanoate-dimer hydrolase activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nylon degradation

Enzyme and pathway databases

UniPathwayiUPA00207.

Names & Taxonomyi

Protein namesi
Recommended name:
6-aminohexanoate-dimer hydrolase (EC:3.5.1.46)
Alternative name(s):
Nylon oligomers-degrading enzyme EII
Gene namesi
Name:nylB
Encoded oniPlasmid pOAD20 Publication
OrganismiFlavobacterium sp. (strain K172)
Taxonomic identifieri261 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeFlavobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3923926-aminohexanoate-dimer hydrolasePRO_0000058011Add
BLAST

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni23 – 275Combined sources
Helixi31 – 355Combined sources
Helixi39 – 413Combined sources
Beta strandi60 – 623Combined sources
Turni67 – 693Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E8IX-ray1.45A1-21[»]
2ZLYX-ray1.58A1-21[»]
2ZM0X-ray1.50A1-21[»]
2ZM2X-ray1.55A1-21[»]
2ZM7X-ray1.60A1-21[»]
2ZM8X-ray1.55A1-21[»]
2ZM9X-ray1.50A1-21[»]
2ZMAX-ray1.51A1-21[»]
3A65X-ray1.70A1-21[»]
3A66X-ray1.60A1-21[»]
3VWLX-ray1.60A1-21[»]
3VWMX-ray1.60A1-21[»]
3VWNX-ray1.20X1-21[»]
3VWPX-ray1.55A1-21[»]
3VWQX-ray1.70A1-21[»]
3VWRX-ray1.65A1-21[»]
ProteinModelPortaliP07061.
SMRiP07061. Positions 5-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07061.

Family & Domainsi

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.

Sequencei

Sequence statusi: Complete.

P07061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNARSTGQHP ARYPGAAAGE PTLDSWQEAP HNRWAFARLG ELLPTAAVSR
60 70 80 90 100
RDPATPAEPV VRLDALATRL PDLEQRLEET CTDAFLVLRG SEVLAEYYRA
110 120 130 140 150
GFAPDDRHLL MSVSKSLCGT VVGALIDEGR IDPAQPVTEY VPELAGSVYD
160 170 180 190 200
GPSVLQVLDM QISIDYNEDY VDPASEVQTH DRSAGWRTRR DGDPADTYEF
210 220 230 240 250
LTTLRGDGGT GEFQYCSANT DVLAWIVERV TGLRYVEALS TYLWAKLDAD
260 270 280 290 300
RDATITVDQT GFGFANGGVS CTARDLARVG RMMLDGGVAP GGRVVSQGWV
310 320 330 340 350
ESVLAGGSRE AMTDEGFTSA FPEGSYTRQW WCTGNERGNV SGIGIHGQNL
360 370 380 390
WLDPRTDSVI VKLSSWPDPD TRHWHGLQSG ILLDVSRALD AV
Length:392
Mass (Da):42,693
Last modified:April 1, 1988 - v1
Checksum:i9CF34C393C3E53D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00046 Genomic DNA. Translation: CAA24927.1.
D26094 Genomic DNA. Translation: BAA05087.1.
PIRiA29516.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00046 Genomic DNA. Translation: CAA24927.1.
D26094 Genomic DNA. Translation: BAA05087.1.
PIRiA29516.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E8IX-ray1.45A1-21[»]
2ZLYX-ray1.58A1-21[»]
2ZM0X-ray1.50A1-21[»]
2ZM2X-ray1.55A1-21[»]
2ZM7X-ray1.60A1-21[»]
2ZM8X-ray1.55A1-21[»]
2ZM9X-ray1.50A1-21[»]
2ZMAX-ray1.51A1-21[»]
3A65X-ray1.70A1-21[»]
3A66X-ray1.60A1-21[»]
3VWLX-ray1.60A1-21[»]
3VWMX-ray1.60A1-21[»]
3VWNX-ray1.20X1-21[»]
3VWPX-ray1.55A1-21[»]
3VWQX-ray1.70A1-21[»]
3VWRX-ray1.65A1-21[»]
ProteinModelPortaliP07061.
SMRiP07061. Positions 5-392.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00207.

Miscellaneous databases

EvolutionaryTraceiP07061.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
SUPFAMiSSF56601. SSF56601. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNYLB_FLASK
AccessioniPrimary (citable) accession number: P07061
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 11, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The EII enzyme is 100 times more active toward the substrate than the EII' enzyme.

Keywords - Technical termi

3D-structure, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.