ID   U7STT2_FUSNU            Unreviewed;       529 AA.
AC   U7STT2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:ERT34596.1};
GN   ORFNames=HMPREF1766_01560 {ECO:0000313|EMBL:ERT34596.1};
OS   Fusobacterium nucleatum CTI-5.
OC   Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=1316586 {ECO:0000313|EMBL:ERT34596.1, ECO:0000313|Proteomes:UP000017135};
RN   [1] {ECO:0000313|EMBL:ERT34596.1, ECO:0000313|Proteomes:UP000017135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTI-5 {ECO:0000313|EMBL:ERT34596.1,
RC   ECO:0000313|Proteomes:UP000017135};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Kostic A., Garrett W.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Gnerre S.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusobacterium nucleatum CTI-5.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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:ERT34596.1}.
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DR   EMBL; AXNW01000021; ERT34596.1; -; Genomic_DNA.
DR   RefSeq; WP_008691832.1; NZ_KI518376.1.
DR   AlphaFoldDB; U7STT2; -.
DR   PATRIC; fig|1316586.3.peg.1522; -.
DR   HOGENOM; CLU_016107_2_1_0; -.
DR   Proteomes; UP000017135; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   CDD; cd01297; D-aminoacylase; 1.
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; 2.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          43..248
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          420..509
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   529 AA;  59463 MW;  C78F32AB65BCADCF CRC64;
     MSTILIKNGT LIDGSGSKRY LADILIENEK IKKIGKLDLT ADKVIDASGK IVSPGFIDTH
     SHSDLKVLIE PFVEPKIRQG ITTEILGQDG ISMAPLPEKY VSSWRKNLAG LDGDSDELKW
     DWKDTNGYLN LISKTGSGPN ELYLVPHGNI RMEAMGLEAR AATKEELEKM KEITRREMEA
     GVAGISTGLI YIPCAYAETE ELIEICKVAA EYGRPLVIHQ RSEADTMLES MQEVIRIAKE
     SGVKIHFSHF KICGQKNWKL IEPVIALLDK CKEEGINISY DQYPYVAGST MLGVILPPWA
     HAGGTDKLIE RLKDKVLREK MKEDIIKGIP GWDNFIDFAG FDGIFVTSVK TNKNQDCIGK
     NLTEIAEMRG KEKFDAVFDL LMEEENAVGM YDYYGKDEHI VTFMKRPESN ICTDGLLGGK
     PHPRVYGSFP RVLGKFVREM QTMVLEEAIY KMTHKPAITF KIENRGLLRE DYFADIVIFD
     ENKIIDKGTF IEPTQFPDGI EYVLVNGKFA VKEGKSTYDL GGKVIRIKR
//