Q59632 (Q59632_OCHAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
D-aminopeptidase EMBL CAA66259.1
EC=3.4.11.19 EMBL CAA66259.1

Gene names

Name:

dmpA EMBL CAA66259.1

Organism

Ochrobactrum anthropi EMBL CAA66259.1

Taxonomic identifier

529 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Ochrobactrum

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Molecular function	Aminopeptidase EMBL CAA66259.1 Hydrolase Protease
Technical term	3D-structure PDB 1B65
Gene Ontology (GO)
Molecular_function	aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	250	1	Nucleophile PDB 1B65
	Site	146	1	Transition state stabilizer; via amide nitrogen PDB 1B65
	Site	218	1	Transition state stabilizer PDB 1B65
	Site	288	1	Important for catalytic activity PDB 1B65
	Site	289	1	Important for catalytic activity; via amide nitrogen PDB 1B65

Sequences

	Sequence		Length	Mass (Da)
	Q59632 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: F91A4EA51AEDAB72	FASTA	375	40,415
	10 20 30 40 50 60 MTSQTPTRKP RARDLGLPFT GVTGPYNAIT DVDGVGVGFQ TIIENEPRPG RKRPARSGVT 70 80 90 100 110 120 AILPHMQSET PVPVYAGVHR FNGNGEMTGT HWIEDGGYFL GPVVITNTHG IGMAHHATVR 130 140 150 160 170 180 WMVDRYASTY QTDDFLWIMP VVAETYDGAL NDINGFPVTE ADVRKALDNV ASGPVQEGNC 190 200 210 220 230 240 GGGTGMITYG FKGGTGTASR VVEFGGRSFT IGALVQANHG QRDWLTIAGV PVGQHMRDGT 250 260 270 280 290 300 PQSQLQERGS IIVVLATDLP LMPHQLKRLA RRASIGIGRN GTPGGNNSGD IFIAFSTANQ 310 320 330 340 350 360 RPMQHRSAPF LDVEMVNDEP LDTVYLAAVD SVEEAVVNAM IAAEDMGGTP FDRLLVQAID 370 HERLRAVLRQ YGRLA

References

[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: LMG7991 EMBL CAA66259.1.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X97669 Genomic DNA. Translation: CAA66259.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B65	X-ray	1.82	A/B/C/D/E/F	1-375	[»]

ProteinModelPortal

Q59632.

SMR

Q59632. Positions 9-375.

ModBase

Search...

Protein family/group databases

MEROPS

P01.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.60.70.12. 1 hit.

InterPro

IPR016117. ArgJ-like_dom.
IPR005321. Peptidase_S58_DmpA.
[Graphical view]

Pfam

PF03576. Peptidase_S58. 1 hit.
[Graphical view]

SUPFAM

SSF56266. Pept_S58_DmpA/Arg_biosyn_ArgJ. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q59632.

Entry information

Entry name

Q59632_OCHAN

Accession

Primary (citable) accession number: Q59632

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)