ID B5GDT6_STRSH Unreviewed; 547 AA.
AC B5GDT6;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=N-acyl-D-amino acid deacylase {ECO:0000313|EMBL:EDY44482.2};
GN ORFNames=SSBG_02087 {ECO:0000313|EMBL:EDY44482.2};
OS Streptomyces sp. (strain SPB074).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465543 {ECO:0000313|EMBL:EDY44482.2, ECO:0000313|Proteomes:UP000002779};
RN [1] {ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Straight P., Clardy J.,
RA Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T., Lander E.,
RA Galagan J., Nusbaum C., Birren B.;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY44482.2, ECO:0000313|Proteomes:UP000002779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPB074 {ECO:0000313|Proteomes:UP000002779};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Streptomyces sp. strain SPB74.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG770539; EDY44482.2; -; Genomic_DNA.
DR RefSeq; WP_008745886.1; NZ_GG770539.1.
DR AlphaFoldDB; B5GDT6; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000002779; 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 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 56..526
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 547 AA; 58149 MW; D8000F01A29DFF12 CRC64;
MPAAAVPSPA PELLVRDALV VDGSGEEPYR ADVLLREGRI AAIGREGGGT RLSAARVLDA
DGLALSPGFI DMHAHSDLAV LRDPAHTAKV AQGVTLEVLG QDGISYAPVD ERTLAEVRRT
IAGWNGGGPG DESVDFDWRT VGEYLDRLDR QGLAVNAAYL VPQGTVRMHA MGWEDRPPTA
AELDRMRQLV AEGMREGAVG MSSGLTYTPG MYAKDAELTA LCRVVAEHGG YYCPHHRSYG
AGALEAYEEM VVLAREADCP LHLAHATMNF GVNEGRAAEL VSLLDGALAA GADISLDTYP
YTPGSTTLAA VLPSWASEGG PEATLARLAD PETAERIRHD LEVVGSDGCH GVPMEWETIE
ISGVTSPGLA GAVGRTVAAS AAARGIAPWS YARELLLADR LGPTILQHVG HEENVRTIMR
HPVHTGGSDG ILQGAKPHPR AYGTFPRYLG TYVRELGVLS LAECVRHLTS RPAARLRLTD
RGLVREGYRA DLVLFDPVTV AAGSTFAEPR TLPAGIPHVL VDGHFVLRDG ARTQATPGRS
VRGRGRR
//
