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Q59632

- Q59632_OCHAN

UniProt

Q59632 - Q59632_OCHAN

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Protein
Submitted name:

D-aminopeptidase

Gene

dmpA

Organism
Ochrobactrum anthropi
Status
Unreviewed - 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 nitrogenImported
Sitei218 – 2181Transition state stabilizerImported
Active sitei250 – 2501NucleophileImported
Sitei288 – 2881Important for catalytic activityImported
Sitei289 – 2891Important for catalytic activity; via amide nitrogenImported

GO - Molecular functioni

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

Keywords - Molecular functioni

AminopeptidaseImported, Hydrolase, Protease

Protein family/group databases

MEROPSiP01.001.

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
Entry Method Resolution (Å) Chain Positions PDBsum
1B65 X-ray 1.82 A/B/C/D/E/F 1-375 [» ]
ProteinModelPortali Q59632.
SMRi Q59632. Positions 9-375.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi P01.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei Q59632.

Family and domain databases

Gene3Di 3.60.70.12. 1 hit.
InterProi IPR016117. ArgJ-like_dom.
IPR005321. Peptidase_S58_DmpA.
[Graphical view ]
Pfami PF03576. Peptidase_S58. 1 hit.
[Graphical view ]
SUPFAMi SSF56266. SSF56266. 1 hit.
ProtoNeti Search...

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(1999) [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(2000) [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: October 29, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3