ID C3K1Y5_PSEFS Unreviewed; 487 AA.
AC C3K1Y5;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=D-aminoacylase {ECO:0000313|EMBL:CAI2799325.1, ECO:0000313|EMBL:CAY52235.1};
DE EC=3.5.1.81 {ECO:0000313|EMBL:CAI2799325.1, ECO:0000313|EMBL:CAY52235.1};
GN OrderedLocusNames=PFLU_5178 {ECO:0000313|EMBL:CAY52235.1};
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY52235.1};
RN [1] {ECO:0000313|EMBL:CAY52235.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAY52235.1};
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
RN [2] {ECO:0000313|EMBL:CAI2799325.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SBW25 {ECO:0000313|EMBL:CAI2799325.1};
RA Fortmann-Grote C.;
RL Submitted (OCT-2023) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OV986001; CAI2799325.1; -; Genomic_DNA.
DR EMBL; AM181176; CAY52235.1; -; Genomic_DNA.
DR RefSeq; WP_015885849.1; NC_012660.1.
DR AlphaFoldDB; C3K1Y5; -.
DR STRING; 294.SRM1_00776; -.
DR PATRIC; fig|216595.4.peg.5310; -.
DR eggNOG; COG3653; Bacteria.
DR HOGENOM; CLU_016107_2_0_6; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP001152918; Chromosome.
DR GO; GO:0047420; F:N-acyl-D-amino-acid deacylase activity; IEA:UniProtKB-EC.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.30.1490.130; 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; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 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 Hydrolase {ECO:0000313|EMBL:CAY52235.1}.
FT DOMAIN 46..459
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 487 AA; 52571 MW; 3727C94AF09622C6 CRC64;
MKYDTLIRQA LIIDGSNTPG YVADVGLRDG RIEAIGDLST AMAEHEIDAA GRVLAPGFID
VHTHDDTVVI RHPQMLPKLS QGVTTVIVGN CGISASPVSL RSDPPDPMNL LGTREAFVYP
RFADYRAAVE SAHPAVNVAA LIGHTALRSN HMDDLHRTAS ADEIAAMRVQ LQESLEAGAL
GLSTGLAYAS AFNAETDEVL QLSEALTAFG AVYTTHLRSE FEPVLEAMDE AFLVGRHAKV
PVIISHLKCA GAGNWGRSPQ LLASLERAAK THPVGCDCYP YAASSSTLDL KQVTDAFRIT
ITWSTPCPAM GGRDLQEIAA EWDVSLMDAA RRLQPAGAVY YGMDEADVRR ILAHPLSMVG
SDGLPEDPFP HPRLWGAFPR VLGHFSRDVG LFPLHTAVHK MTGLSAARFG LADRGEVREG
HWADLVLFDP LRVRDVADFK EPQRAAEGID GVWVNGVLSY SDGQANGQRP GRFLARSGDL
RRGFSSL
//
