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Protein
Submitted name:

Carboxyl esterase NP

Gene

nap

Organism
Bacillus subtilis
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseImported

Protein family/group databases

ESTHERibacsu-cbxnp. 6_AlphaBeta_hydrolase.

Names & Taxonomyi

Protein namesi
Submitted name:
Carboxyl esterase NPImported
Submitted name:
Carboxylesterase NPImported (EC:3.1.1.1Imported)
Gene namesi
Name:napImported
OrganismiBacillus subtilisImported
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003063.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CCWX-ray1.75A2-300[»]
SMRiQ59248. Positions 7-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 286229AB_hydrolase_1InterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiENOG4108WC5. Bacteria.
COG0596. LUCA.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNHSSSIPE LSDNGIRYYQ TYNESLSLWP VRCKSFYIST RFGQTHVIAS
60 70 80 90 100
GPEDAPPLVL LHGALFSSTM WYPNIADWSS KYRTYAVDII GDKNKSIPEN
110 120 130 140 150
LSGTRTDYAN WLLDVFDNLG IEKSHMIGLS LGGLHTMNFL LRMPERVKSA
160 170 180 190 200
AILSPAETFL PFHHDFYKYA LGLTASNGVE KFLNWMMTDQ NVLHPIFVKQ
210 220 230 240 250
FQAGVMWQDG SRNPNPKADG FPYVFTDEEL RSARVPILLL LGEHEVIYDP
260 270 280 290 300
HSALHRASSF VPDIEAEVIK NAGHVLSMEQ PAYVNERVMR FFNAETGISR
Length:300
Mass (Da):33,966
Last modified:November 1, 1996 - v1
Checksum:i4140BC256C794107
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17574 Genomic DNA. Translation: AAC43262.1.
X82892 Genomic DNA. Translation: CAA58063.1.
PIRiI40425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17574 Genomic DNA. Translation: AAC43262.1.
X82892 Genomic DNA. Translation: CAA58063.1.
PIRiI40425.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CCWX-ray1.75A2-300[»]
SMRiQ59248. Positions 7-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003063.

Protein family/group databases

ESTHERibacsu-cbxnp. 6_AlphaBeta_hydrolase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108WC5. Bacteria.
COG0596. LUCA.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
[Graphical view]
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Development of a new Bacillus carboxyl esterase for use in the resolution of chiral drugs."
    Quax W.J., Broekhuizen C.P.
    Appl. Microbiol. Biotechnol. 41:425-431(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ThaiI-8Imported.
  2. "Crystal structures of two Bacillus carboxylesterases with different enantioselectivities."
    Rozeboom H.J., Godinho L.F., Nardini M., Quax W.J., Dijkstra B.W.
    Biochim. Biophys. Acta 1844:567-575(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 2-300.

Entry informationi

Entry nameiQ59248_BACIU
AccessioniPrimary (citable) accession number: Q59248
Secondary accession number(s): Q53426, Q59221
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.