ID A0A2N7X3Q9_9BURK Unreviewed; 488 AA.
AC A0A2N7X3Q9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=D-aminoacylase {ECO:0000313|EMBL:PMS36383.1};
GN ORFNames=C0Z20_12975 {ECO:0000313|EMBL:PMS36383.1};
OS Trinickia symbiotica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=863227 {ECO:0000313|EMBL:PMS36383.1, ECO:0000313|Proteomes:UP000235777};
RN [1] {ECO:0000313|EMBL:PMS36383.1, ECO:0000313|Proteomes:UP000235777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPY 581 {ECO:0000313|EMBL:PMS36383.1,
RC ECO:0000313|Proteomes:UP000235777};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-2018) 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:PMS36383.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PNYC01000007; PMS36383.1; -; Genomic_DNA.
DR RefSeq; WP_018443689.1; NZ_PTIR01000007.1.
DR AlphaFoldDB; A0A2N7X3Q9; -.
DR STRING; 863227.GCA_000373005_05075; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000235777; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000235777}.
FT DOMAIN 50..462
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 488 AA; 52551 MW; 58B0532A53135B1B CRC64;
MHSHPEAADT LIVGAQLYDG TGEPPVVRDV AVRDGRIAAI GNLSNWLAEE VVEAEGRALA
PGFIDVHTHD DTHVIRSPQC LPKITQGVTT VIVGNCGISA SPVTLKGDPP DPMNLLGERD
AFRYPTFAAY VDAIEAARPA VNVAALIGHT ALRNNHMDRL DRAATERELA AMRAELEEAL
AHGALGLSSG LAYASANAAP TEEVMALAEP LAAAGAVYTT HMRSEFDAIL EAFDEACRIG
RHARVPVVVS HLKCAGPSNW GRSKEVLASL EAARRIQPIG CDCYPYDRSS STLDLKQVTG
DIEITITWST PHPEQAGKRI SAIAAEWGVN EREAAERLQP AGAVYHNMSE DDVRRILSHP
ATMIGSDGLP NDPLPHPRLW GAFPRVLGHY ARDAKLIPLE EAVRKMTSLS AQRFGLGPRG
EVRVGFQADL VLFDPARIRD AATFENPRQA ADGIDAVWVN GVLSCRNGEA TGERAGRFVA
RGATWREQ
//