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Protein

6-aminohexanoate-dimer hydrolase

Gene

nylB'

Organism
Flavobacterium sp. (strain K172)
Status
Reviewed-Annotation score: Annotation score: 2 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 – 1121By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nylon degradation

Enzyme and pathway databases

BRENDAi3.5.1.46. 2302.
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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi181 – 1811G → D: Enhances activity. 1 Publication
Mutagenesisi266 – 2661H → N: Enhances activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3923926-aminohexanoate-dimer hydrolasePRO_0000058012Add
BLAST

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni23 – 275Combined sources
Turni29 – 313Combined sources
Helixi32 – 354Combined sources
Helixi39 – 413Combined sources
Beta strandi60 – 623Combined sources
Helixi66 – 694Combined sources
Helixi73 – 797Combined sources
Beta strandi82 – 898Combined sources
Beta strandi92 – 987Combined sources
Helixi113 – 12715Combined sources
Helixi137 – 1404Combined sources
Helixi142 – 1443Combined sources
Helixi154 – 1585Combined sources
Helixi176 – 1838Combined sources
Helixi197 – 2026Combined sources
Beta strandi210 – 2123Combined sources
Helixi217 – 23115Combined sources
Helixi235 – 2428Combined sources
Helixi244 – 2463Combined sources
Turni265 – 2673Combined sources
Beta strandi269 – 2713Combined sources
Helixi273 – 28412Combined sources
Turni285 – 2873Combined sources
Helixi297 – 3059Combined sources
Helixi309 – 3113Combined sources
Helixi315 – 3184Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi340 – 3445Combined sources
Turni345 – 3473Combined sources
Beta strandi348 – 3536Combined sources
Helixi354 – 3563Combined sources
Beta strandi358 – 3647Combined sources
Beta strandi367 – 3693Combined sources
Helixi372 – 38817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYBX-ray1.80A6-392[»]
1WYCX-ray1.58A9-392[»]
2DCFX-ray1.40A9-392[»]
2E8IX-ray1.45A22-392[»]
2ZLYX-ray1.58A22-392[»]
2ZM0X-ray1.50A22-392[»]
2ZM2X-ray1.55A22-392[»]
2ZM7X-ray1.60A22-392[»]
2ZM8X-ray1.55A22-392[»]
2ZM9X-ray1.50A22-392[»]
2ZMAX-ray1.51A22-392[»]
3A65X-ray1.70A22-392[»]
3A66X-ray1.60A22-392[»]
3VWLX-ray1.60A22-392[»]
3VWMX-ray1.60A22-392[»]
3VWNX-ray1.20X22-392[»]
3VWPX-ray1.55A22-392[»]
3VWQX-ray1.70A22-392[»]
3VWRX-ray1.65A22-392[»]
ProteinModelPortaliP07062.
SMRiP07062. Positions 5-392.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07062.

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.

P07062-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTPTTGSHP ARYPSAAAGE PTLDSWQEPP HNRWAFAHLG EMVPSAAVSR
60 70 80 90 100
RPVNAPGHAL ARLGAIAAQL PDLEQRLEQT YTDAFLVLRG TEVVAEYYRA
110 120 130 140 150
GFAPDDRHLL MSVSKSLCGT VVGALVDEGR IDPAQPVTEY VPELAGSVYD
160 170 180 190 200
GPSVLQVLDM QISIDYNEDY VDPASEVQTH GRSAGWRTRA TGDPADTYEF
210 220 230 240 250
LTTLRGDGST GEFQYCSANT DVLAWIVERV TGLRYVEALS TYLWAKLDAD
260 270 280 290 300
RDATITVDTT GFGFAHGGVS CTARDLARVG RMMLDGGVAP GGRVVSEDWV
310 320 330 340 350
RRVLAGGSHE AMTDKGFTNT FPDGSYTRQW WCTGNERGNV SGIGIHGQNL
360 370 380 390
WLDPLTDSVI VKLSSWPDPD TEHWHRLQNG ILLDVSRALD AV
Length:392
Mass (Da):42,647
Last modified:April 1, 1988 - v1
Checksum:i527E585107B35EA2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02864 Genomic DNA. Translation: CAA26616.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02864 Genomic DNA. Translation: CAA26616.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYBX-ray1.80A6-392[»]
1WYCX-ray1.58A9-392[»]
2DCFX-ray1.40A9-392[»]
2E8IX-ray1.45A22-392[»]
2ZLYX-ray1.58A22-392[»]
2ZM0X-ray1.50A22-392[»]
2ZM2X-ray1.55A22-392[»]
2ZM7X-ray1.60A22-392[»]
2ZM8X-ray1.55A22-392[»]
2ZM9X-ray1.50A22-392[»]
2ZMAX-ray1.51A22-392[»]
3A65X-ray1.70A22-392[»]
3A66X-ray1.60A22-392[»]
3VWLX-ray1.60A22-392[»]
3VWMX-ray1.60A22-392[»]
3VWNX-ray1.20X22-392[»]
3VWPX-ray1.55A22-392[»]
3VWQX-ray1.70A22-392[»]
3VWRX-ray1.65A22-392[»]
ProteinModelPortaliP07062.
SMRiP07062. Positions 5-392.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00207.
BRENDAi3.5.1.46. 2302.

Miscellaneous databases

EvolutionaryTraceiP07062.

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 nameiNYLC_FLASK
AccessioniPrimary (citable) accession number: P07062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: October 14, 2015
This is version 82 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.