ID   Q59632_BRUAN            Unreviewed;       375 AA.
AC   Q59632;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   04-NOV-2026, entry version 104.
DE   SubName: Full=D-aminopeptidase {ECO:0000313|EMBL:CAA66259.1};
DE            EC=3.4.11.19 {ECO:0000313|EMBL:CAA66259.1};
GN   Name=dmpA {ECO:0000313|EMBL:CAA66259.1};
OS   Brucella anthropi (Ochrobactrum anthropi).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=529 {ECO:0000313|EMBL:CAA66259.1};
RN   [1] {ECO:0000313|EMBL:CAA66259.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LMG7991 {ECO:0000313|EMBL:CAA66259.1};
RX   PubMed=10379365; DOI=10.1007/s000180050334;
RA   Fanuel L.C.I., Thamm I., Kostanjevecki V., Samyn B., Joris B., Goffin C.,
RA   Brannigan J., Van Beeumen J., Frere J.M.;
RT   "Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-
RT   nitroanilide.";
RL   Cell. Mol. Life Sci. 55:812-818(1999).
RN   [2] {ECO:0007829|PDB:1B65}
RP   X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS), AND ACTIVE SITE.
RX   PubMed=10673442; DOI=10.1016/s0969-2126(00)00091-5;
RA   Bompard-Gilles C., Villeret V., Davies G.J., Fanuel L., Joris B.,
RA   Frere J.M., Van Beeumen J.;
RT   "A new variant of the Ntn hydrolase fold revealed by the crystal structure
RT   of L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi.";
RL   Structure 8:153-162(2000).
CC   -!- SIMILARITY: Belongs to the peptidase S58 family.
CC       {ECO:0000256|ARBA:ARBA00007068}.
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DR   EMBL; X97669; CAA66259.1; -; Genomic_DNA.
DR   RefSeq; WP_043062538.1; NZ_JACGXF010000009.1.
DR   PDB; 1B65; X-ray; 1.82 A; A/B/C/D/E/F=1-375.
DR   SMR; Q59632; -.
DR   MEROPS; P01.001; -.
DR   PATRIC; fig|529.8.peg.3028; -.
DR   BRENDA; 3.4.13.20; 4382.
DR   EvolutionaryTrace; Q59632; -.
DR   CDD; cd02253; DmpA; 1.
DR   Gene3D; 3.60.70.12; L-amino peptidase D-ALA esterase/amidase; 1.
DR   InterPro; IPR016117; ArgJ-like_dom_sf.
DR   InterPro; IPR005321; Peptidase_S58_DmpA.
DR   PANTHER; PTHR36512:SF3; BLR5678 PROTEIN; 1.
DR   PANTHER; PTHR36512; D-AMINOPEPTIDASE; 1.
DR   Pfam; PF03576; Peptidase_S58; 1.
DR   SUPFAM; SSF56266; DmpA/ArgJ-like; 1.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:TreeGrafter.
DR   AlphaFoldDB; Q59632; -.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1B65};
KW   Aminopeptidase {ECO:0000313|EMBL:CAA66259.1};
KW   Hydrolase {ECO:0000313|EMBL:CAA66259.1};
KW   Protease {ECO:0000313|EMBL:CAA66259.1}.
FT   ACT_SITE        250
FT                   /note="Nucleophile, Proton donor/acceptor"
FT                   /evidence="ECO:0007829|PDB:1B65"
SQ   SEQUENCE   375 AA;  40415 MW;  F91A4EA51AEDAB72 CRC64;
     MTSQTPTRKP RARDLGLPFT GVTGPYNAIT DVDGVGVGFQ TIIENEPRPG RKRPARSGVT
     AILPHMQSET PVPVYAGVHR FNGNGEMTGT HWIEDGGYFL GPVVITNTHG IGMAHHATVR
     WMVDRYASTY QTDDFLWIMP VVAETYDGAL NDINGFPVTE ADVRKALDNV ASGPVQEGNC
     GGGTGMITYG FKGGTGTASR VVEFGGRSFT IGALVQANHG QRDWLTIAGV PVGQHMRDGT
     PQSQLQERGS IIVVLATDLP LMPHQLKRLA RRASIGIGRN GTPGGNNSGD IFIAFSTANQ
     RPMQHRSAPF LDVEMVNDEP LDTVYLAAVD SVEEAVVNAM IAAEDMGGTP FDRLLVQAID
     HERLRAVLRQ YGRLA
//