ID W2ET71_9ACTN Unreviewed; 533 AA.
AC W2ET71;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=N-acyl-D-amino acid deacylase {ECO:0000313|EMBL:ETK34131.1};
GN ORFNames=MPTA5024_21230 {ECO:0000313|EMBL:ETK34131.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK34131.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK34131.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK34131.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETK34131.1}.
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DR EMBL; AWEV01000156; ETK34131.1; -; Genomic_DNA.
DR RefSeq; WP_036325795.1; NZ_KI866523.1.
DR AlphaFoldDB; W2ET71; -.
DR STRING; 316330.MPTA5024_21230; -.
DR PATRIC; fig|316330.3.peg.4098; -.
DR HOGENOM; CLU_016107_2_1_11; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000018869; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR013108; Amidohydro_3.
DR InterPro; IPR023100; D-aminoacylase_insert_dom_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018869}.
FT DOMAIN 46..517
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 533 AA; 55073 MW; B307D432AB76C7AF CRC64;
MSRADLLVRG GVLVDGTGAP GRPADVAVTG GRLAVLPPGA AVEAAEVLDA RGRIVAPGFV
DVHTHSDGAA LLGEADAGRA LVRAAVLQGV TTEICGNCGS GLFPALPSQL PAMRAEARVT
FGGDTGMFRD FAGFAAAHTA AGRANNVASL VGHGTLRSGV LGPVDRPARP EELREMCALL
DLALSQGAAG LSTGLIYTPG SYAGTDEVVA LAAVAARHGK PYVTHLRDEM SRVEEALEEA
VEISVRSGAA LHVSHHKTAG RYAWGRTERT LPRIAALRAA GMDVTCDVYP YTAASTALSA
MLPPWANDGG LAALAARLGD PAQRDRMRRA IAEGVPGWEN TVGNGGWDRI SVACAPRHPQ
TEGRTIAELA AAASADPLDT AAGLLVAERG EVTIISHSMV EEDVRRVLAA PYAMIGSDGV
PKPGGRPHPR WAGTFPRVLG RYARELGLLT LEEAVHKMTG MAAARFGLAG RGVVRDGAHA
DLVVFDAERV ADRATFTDPL LPPEGIEAVV VAGAVVVRDG EETGARPGQV LTT
//
