ID D9QSU9_ACEAZ Unreviewed; 527 AA.
AC D9QSU9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:ADL11637.1};
DE EC=3.5.1.81 {ECO:0000313|EMBL:ADL11637.1};
GN OrderedLocusNames=Acear_0086 {ECO:0000313|EMBL:ADL11637.1};
OS Acetohalobium arabaticum (strain ATCC 49924 / DSM 5501 / Z-7288).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Acetohalobium.
OX NCBI_TaxID=574087 {ECO:0000313|EMBL:ADL11637.1, ECO:0000313|Proteomes:UP000001661};
RN [1] {ECO:0000313|EMBL:ADL11637.1, ECO:0000313|Proteomes:UP000001661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49924 / DSM 5501 / Z-7288
RC {ECO:0000313|Proteomes:UP000001661};
RX PubMed=21304692;
RA Sikorski J., Lapidus A., Chertkov O., Lucas S., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Brambilla E.,
RA Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA Bruce D., Detter C., Tapia R., Goodwin L., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M.,
RA Spring S., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acetohalobium arabaticum type strain (Z-
RT 7288).";
RL Stand. Genomic Sci. 3:57-65(2010).
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DR EMBL; CP002105; ADL11637.1; -; Genomic_DNA.
DR RefSeq; WP_013277084.1; NC_014378.1.
DR AlphaFoldDB; D9QSU9; -.
DR STRING; 574087.Acear_0086; -.
DR KEGG; aar:Acear_0086; -.
DR eggNOG; COG3653; Bacteria.
DR HOGENOM; CLU_016107_2_1_9; -.
DR OrthoDB; 9775607at2; -.
DR Proteomes; UP000001661; 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; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF6; AMIDOHYDROLASE-RELATED; 1.
DR Pfam; PF07969; Amidohydro_3; 2.
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:ADL11637.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001661}.
FT DOMAIN 48..215
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 416..510
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 527 AA; 58195 MW; 3D9E6DDFBD550730 CRC64;
MKLDLKLSGG TVVDGTGRDR FRTDIGIKDG EIVKLGDLKE LNACIEYNIE GLIIAPGFID
IHSHSKYSIL ANPKASGKVY QGVTTEVVGN CGSSAAPVTD RSTEAVQDSL DKYNLELEWQ
SFAGYFGVLE KKGTALNIAS LVGHGLLRKS VMGDEPRRPT NDELIEMKQL LASALEDGAW
GLSTGLIYPP SSYAATEELM ELAQVAAEYN GIYSTHLRSE GDELIKAVKE AIKIGRETGV
SVEISHHKAI GKNNWGKVDK TLELITKARD EGFNISCDMY PYLATSTGLA ALLPAKIKEG
GKEKVLRRLQ NKKSVAEIKQ YWQQKQQPKD YWSKILISEV SSDDNQHLEG KSITQIAERR
NQKPADIVIK LLIEEELQIS MVKFSISEAD LKKVLEFPET MISSDSLTRV KDGLLDQGKP
HPRAYGSFPR VIDKFVKDKE LLTLEEAVKK MSYLPAQKLG LNNRGEIAVG KKADLAVFDL
TEFTDQATYK QPHRYAAGLK YLIINGQPVV EDAEQTSALP GRVLINL
//
