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Protein
Submitted name:

D-aminopeptidase

Gene

dmpA

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

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei146 – 1461Transition state stabilizer; via amide nitrogenCombined sources
Sitei218 – 2181Transition state stabilizerCombined sources
Active sitei250 – 2501NucleophileCombined sources
Sitei288 – 2881Important for catalytic activityCombined sources
Sitei289 – 2891Important for catalytic activity; via amide nitrogenCombined sources

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

AminopeptidaseImported, Hydrolase, Protease

Enzyme and pathway databases

BRENDAi3.4.13.20. 4382.

Names & Taxonomyi

Protein namesi
Submitted name:
D-aminopeptidaseImported (EC:3.4.11.19Imported)
Gene namesi
Name:dmpAImported
OrganismiOchrobactrum anthropiImported
Taxonomic identifieri529 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B65X-ray1.82A/B/C/D/E/F1-375[»]
ProteinModelPortaliQ59632.
SMRiQ59632. Positions 9-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59632.

Family & Domainsi

Family and domain databases

Gene3Di3.60.70.12. 1 hit.
InterProiIPR016117. ArgJ-like_dom.
IPR005321. Peptidase_S58_DmpA.
[Graphical view]
PfamiPF03576. Peptidase_S58. 1 hit.
[Graphical view]
SUPFAMiSSF56266. SSF56266. 1 hit.

Sequencei

Sequence statusi: Complete.

Q59632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSQTPTRKP RARDLGLPFT GVTGPYNAIT DVDGVGVGFQ TIIENEPRPG
60 70 80 90 100
RKRPARSGVT AILPHMQSET PVPVYAGVHR FNGNGEMTGT HWIEDGGYFL
110 120 130 140 150
GPVVITNTHG IGMAHHATVR WMVDRYASTY QTDDFLWIMP VVAETYDGAL
160 170 180 190 200
NDINGFPVTE ADVRKALDNV ASGPVQEGNC GGGTGMITYG FKGGTGTASR
210 220 230 240 250
VVEFGGRSFT IGALVQANHG QRDWLTIAGV PVGQHMRDGT PQSQLQERGS
260 270 280 290 300
IIVVLATDLP LMPHQLKRLA RRASIGIGRN GTPGGNNSGD IFIAFSTANQ
310 320 330 340 350
RPMQHRSAPF LDVEMVNDEP LDTVYLAAVD SVEEAVVNAM IAAEDMGGTP
360 370
FDRLLVQAID HERLRAVLRQ YGRLA
Length:375
Mass (Da):40,415
Last modified:November 1, 1996 - v1
Checksum:iF91A4EA51AEDAB72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97669 Genomic DNA. Translation: CAA66259.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97669 Genomic DNA. Translation: CAA66259.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B65X-ray1.82A/B/C/D/E/F1-375[»]
ProteinModelPortaliQ59632.
SMRiQ59632. Positions 9-375.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.13.20. 4382.

Miscellaneous databases

EvolutionaryTraceiQ59632.

Family and domain databases

Gene3Di3.60.70.12. 1 hit.
InterProiIPR016117. ArgJ-like_dom.
IPR005321. Peptidase_S58_DmpA.
[Graphical view]
PfamiPF03576. Peptidase_S58. 1 hit.
[Graphical view]
SUPFAMiSSF56266. SSF56266. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-nitroanilide."
    Fanuel L.C.I., Thamm I., Kostanjevecki V., Samyn B., Joris B., Goffin C., Brannigan J., Van Beeumen J., Frere J.M.
    Cell. Mol. Life Sci. 55:812-818(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: LMG7991Imported.
  2. "A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi."
    Bompard-Gilles C., Villeret V., Davies G.J., Fanuel L., Joris B., Frere J.M., Van Beeumen J.
    Structure 8:153-162(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS), ACTIVE SITE.

Entry informationi

Entry nameiQ59632_OCHAN
AccessioniPrimary (citable) accession number: Q59632
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 1, 2015
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.