ID A0A1V0DG57_9BACT Unreviewed; 537 AA.
AC A0A1V0DG57;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:ARA94004.1};
GN ORFNames=AWN76_013130 {ECO:0000313|EMBL:ARA94004.1};
OS Rhodothermaceae bacterium RA.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae.
OX NCBI_TaxID=1779382 {ECO:0000313|EMBL:ARA94004.1, ECO:0000313|Proteomes:UP000055617};
RN [1] {ECO:0000313|EMBL:ARA94004.1, ECO:0000313|Proteomes:UP000055617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA {ECO:0000313|EMBL:ARA94004.1,
RC ECO:0000313|Proteomes:UP000055617};
RA Liew K.J.;
RT "Complete genome of the potential lignocellulosic biomass degrader
RT Rhodothermaceae bacterium RA isolated from the saline hot spring in
RT Malaysia.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP020382; ARA94004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0DG57; -.
DR STRING; 1779382.AWN76_013130; -.
DR KEGG; rbar:AWN76_013130; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000055617; Chromosome.
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; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR PANTHER; PTHR11113:SF16; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000055617}.
FT DOMAIN 69..513
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT REGION 516..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 56724 MW; 893591418B885A5B CRC64;
MSPRWLLSVL LVLITGCGEA PITGHFDVIL AGGTVYDGLG TPGRVADVAF RADTIAAIGD
LRRATADTVL DVAGLAVVPG FIDIHSHALG STVEQSALVR RPEAENYVRQ GVTTVLGGQD
GSSAVPVAPL LQALEARPPA VNVGTFVGHG SVRAFVMGNV DRAPTPAELD RMKALVADAM
AAGAFGLSSG LEYTPGAFAG TDELVALARE IAPYDGLYIS HVRDEGGRLL ESVEEVIAVG
EGAGVKAQVT HHKLIGKHRW GGSAASLARI DEARRRGVDV ASDQYPYTAS STGMTILFPS
WSLEGRRADR LARLRDPATR ARIRDAIVEH LERERGGDPA TVVAASCPFD PSLNGQSLAD
ILAARGRAVT LPNAAELAME LLERGGCQGV FHSMGEEDVR RIMQHPMTMI ASDGGVPAPG
EGVPHPRNYG TFARVLAHYV RDEQVLSFEE AVRKMTSLPA SRLGLADRGV LRVGARADVT
VLDPATVQDH ATFTEPHRYA TGVVHVFVNG TAVLRDGEPT GARPGQVLRN PRAHAGR
//
