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Database: UniProt
Entry: A0A101MYN8_9ACTN
LinkDB: A0A101MYN8_9ACTN
Original site: A0A101MYN8_9ACTN 
ID   A0A101MYN8_9ACTN        Unreviewed;       576 AA.
AC   A0A101MYN8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Aminoacylase {ECO:0000313|EMBL:KUM83289.1};
GN   ORFNames=AQI94_37135 {ECO:0000313|EMBL:KUM83289.1};
OS   Streptomyces pseudovenezuelae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM83289.1, ECO:0000313|Proteomes:UP000053039};
RN   [1] {ECO:0000313|EMBL:KUM83289.1, ECO:0000313|Proteomes:UP000053039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM83289.1,
RC   ECO:0000313|Proteomes:UP000053039};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT   strain for the species Streptomyces pseudovenezuelae.";
RL   Submitted (OCT-2015) 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:KUM83289.1}.
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DR   EMBL; LMWM01000045; KUM83289.1; -; Genomic_DNA.
DR   RefSeq; WP_031039898.1; NZ_KQ948153.1.
DR   AlphaFoldDB; A0A101MYN8; -.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000053039; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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; 2.
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; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
FT   DOMAIN          45..547
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   576 AA;  62025 MW;  CA38350AC1B71558 CRC64;
     MLDHVIKGAT VVDGTGAAAF TADVGIRDGR IAAIGELTEE ARTAEDAAGL VLAPGFVDPH
     THYDAQLFWD PYATPSLNHG VTTVAAGNCG FTLAPLNPAR PEDADYTRRM MSKVEGMSLV
     ALEEGAPWSW SSFGEYLDAL EGRIAVNAGF MVGHCALRRY VMGPDAVGGQ PSEDQLAQML
     RLFHEAMEAG AWGFSTTQSS THSDGDGKPV ASRHALPAEL LALSRAVGEH EGTQIEAIVA
     GCLDQFSDAE IDLFVEMSAA AGRPLNWNVL TIDSSVPERV PRQLFASEQA RKAGGRVVAL
     TMPILTPMNM SLGTFCALNL IPGWGPVLAL PVPERIERLR DPDVQRELLR QSQAKEAGVF
     RRLTNFGRYV IGDTYSDANR GLSGRVVQDI AAERGQEPFA ALVEICAADD LRTVLWPMPT
     DNDPASWAMR AEAWQHEDVL LGGSDAGAHL DRMCGAPYTT RFLGDCLRGR KLTSLEQAVK
     MLTDDPARLF GLRGRGRIEE GFHADLVLFD PERIAAGTAT LVHDLPGDSP RLDSKAIGIR
     AVWVNGVEAI RDDVVSGAVP GRVLRSGRDT RTVSTR
//
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