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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)DescriptionActionsGraphical viewLength
Active sitei112By similarity1

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)DescriptionActionsGraphical viewLength
Mutagenesisi181G → D: Enhances activity. 1 Publication1
Mutagenesisi266H → N: Enhances activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000580121 – 3926-aminohexanoate-dimer hydrolaseAdd BLAST392

Structurei

Secondary structure

1392
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni23 – 27Combined sources5
Turni29 – 31Combined sources3
Helixi32 – 35Combined sources4
Helixi39 – 41Combined sources3
Beta strandi60 – 62Combined sources3
Helixi66 – 69Combined sources4
Helixi73 – 79Combined sources7
Beta strandi82 – 89Combined sources8
Beta strandi92 – 98Combined sources7
Helixi113 – 127Combined sources15
Helixi137 – 140Combined sources4
Helixi142 – 144Combined sources3
Helixi154 – 158Combined sources5
Helixi176 – 183Combined sources8
Helixi197 – 202Combined sources6
Beta strandi210 – 212Combined sources3
Helixi217 – 231Combined sources15
Helixi235 – 242Combined sources8
Helixi244 – 246Combined sources3
Turni265 – 267Combined sources3
Beta strandi269 – 271Combined sources3
Helixi273 – 284Combined sources12
Turni285 – 287Combined sources3
Helixi297 – 305Combined sources9
Helixi309 – 311Combined sources3
Helixi315 – 318Combined sources4
Beta strandi325 – 327Combined sources3
Beta strandi330 – 332Combined sources3
Beta strandi340 – 344Combined sources5
Turni345 – 347Combined sources3
Beta strandi348 – 353Combined sources6
Helixi354 – 356Combined sources3
Beta strandi358 – 364Combined sources7
Beta strandi367 – 369Combined sources3
Helixi372 – 388Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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: November 2, 2016
This is version 84 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.