ID   E8V0L2_TERSS            Unreviewed;       519 AA.
AC   E8V0L2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:ADV81075.1};
DE            EC=3.5.1.81 {ECO:0000313|EMBL:ADV81075.1};
GN   OrderedLocusNames=AciPR4_0237 {ECO:0000313|EMBL:ADV81075.1};
OS   Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV81075.1, ECO:0000313|Proteomes:UP000006844};
RN   [1] {ECO:0000313|EMBL:ADV81075.1, ECO:0000313|Proteomes:UP000006844}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC   {ECO:0000313|Proteomes:UP000006844};
RX   PubMed=23450133; DOI=10.4056/sigs.3036810;
RA   Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA   Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT   "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT   an Acidobacteria from tundra soil.";
RL   Stand. Genomic Sci. 7:59-69(2012).
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DR   EMBL; CP002467; ADV81075.1; -; Genomic_DNA.
DR   RefSeq; WP_013566808.1; NC_014963.1.
DR   AlphaFoldDB; E8V0L2; -.
DR   STRING; 401053.AciPR4_0237; -.
DR   KEGG; tsa:AciPR4_0237; -.
DR   eggNOG; COG3653; Bacteria.
DR   HOGENOM; CLU_016107_2_1_0; -.
DR   Proteomes; UP000006844; Chromosome.
DR   GO; GO:0047420; F:N-acyl-D-amino-acid deacylase activity; IEA:UniProtKB-EC.
DR   CDD; cd01297; D-aminoacylase; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
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; 2.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ADV81075.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006844};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..519
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003232259"
FT   DOMAIN          72..212
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          378..502
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   519 AA;  55631 MW;  D9979894FFA1E35A CRC64;
     MTASLKYLLA RVFVVSSFPL IAVAAQSQDL DVIVRGGSVL DGSGSAAVKT DVGIKGDRIV
     FVGPSKGHKA KRVIDATGLV VTPGFIDPHT HTAEDLSNPM YSRNDAYLMQ GVTTVVTGND
     GSSPTDVGAT LARWKRQGIG TNAALFIGQG TVRSEVMAMS DAKPTPEQME KMKSLVETAM
     SEGAIGLSTG LYYAPGSYSS TEEVIELAKI AARHGGLYDT HMRDESSYNI GLLGSVRETI
     RIGRETQMPV MISHIKALGA DVWGQSSDVI ALIDAARKDG VKVTASQYPY TASGTSVTAS
     LVPRWAEVGG HNALLKNMTD PSVHAHLVEE MTLNLKRRGG PEALLMTSAK DKSIVGKTLE
     TIAAERKVSP IDAAIQIVLA GGSDVASFNM KEADIEAFMR QPWVMTCSDG SEGHPRKFGT
     FPRKLREYVY QRHVISLEFA VRSSTSLTAE TLGLKERGLL KPGYFADVLV FDPKTFNERA
     TYQSPRVLAT GVRYLTVNGV LVINNGALTT ALAGRPLKH
//