ID D5RR22_9PROT Unreviewed; 483 AA.
AC D5RR22;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:EFH10245.1};
DE EC=3.5.1.81 {ECO:0000313|EMBL:EFH10245.1};
GN Name=dan {ECO:0000313|EMBL:EFH10245.1};
GN ORFNames=HMPREF0731_3534 {ECO:0000313|EMBL:EFH10245.1};
OS Pseudoroseomonas cervicalis ATCC 49957.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Pseudoroseomonas.
OX NCBI_TaxID=525371 {ECO:0000313|EMBL:EFH10245.1, ECO:0000313|Proteomes:UP000005324};
RN [1] {ECO:0000313|EMBL:EFH10245.1, ECO:0000313|Proteomes:UP000005324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49957 {ECO:0000313|EMBL:EFH10245.1,
RC ECO:0000313|Proteomes:UP000005324};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (APR-2010) 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:EFH10245.1}.
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DR EMBL; ADVL01000683; EFH10245.1; -; Genomic_DNA.
DR RefSeq; WP_007002564.1; NZ_GG770777.1.
DR AlphaFoldDB; D5RR22; -.
DR HOGENOM; CLU_016107_2_0_5; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000005324; Unassembled WGS sequence.
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:EFH10245.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005324}.
FT DOMAIN 51..463
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 483 AA; 52468 MW; DB9158D329829A2F CRC64;
MALRCDMIIR DATLFDGTGG PRRVGDVGVV GDRIVGVGDL GGMSADREVI ATGKALAPGF
IDAHTHDDRA VLCGPACTLC KISQGVTTVV VGNCGISLAP MRHTDKRPPA PLDLLGDEQW
WTFDSFGDYA HALKTKGSEV NTYALIGHQT LRVEAMGGDP YRAATDAEIL RMQTRLKQAL
AEGGSGFSTG LYYAPNAKAS AEEVVAVGEA MRTMGGLYVT HMRDEADFIC ASIEETLKIA
RRIGVPAHIS HHKCSMPENY GRSVQTLALI QAAASMQEVA FDVYPYPAGS TVLMPDRVRD
DLRTIITWSV PYPEMAGKDL SEIARGWNTD LRAAAERLTP AGAVTFQMDE EDVRRIMRHP
LSMIGSDGLP HDEKPHPRLW GTFPRVLGFY TRQLGLFDME TAIHKMTGRA AQVFGMVDRG
VLREGAYADL VLFDPNTVMD NATFENPVQM SVGIEQVWAN GVATFAAGKE TGEKPGRLVT
RNR
//
