ID H6NKM9_9BACL Unreviewed; 534 AA.
AC H6NKM9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=D-aminoacylase {ECO:0000313|EMBL:AFC33166.1};
GN ORFNames=PM3016_6541 {ECO:0000313|EMBL:AFC33166.1};
OS Paenibacillus mucilaginosus 3016.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1116391 {ECO:0000313|EMBL:AFC33166.1, ECO:0000313|Proteomes:UP000007523};
RN [1] {ECO:0000313|EMBL:AFC33166.1, ECO:0000313|Proteomes:UP000007523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3016 {ECO:0000313|EMBL:AFC33166.1,
RC ECO:0000313|Proteomes:UP000007523};
RX PubMed=22535950; DOI=10.1128/JB.00323-12;
RA Ma M., Wang Z., Li L., Jiang X., Guan D., Cao F., Chen H., Wang X.,
RA Shen D., Du B., Li J.;
RT "Complete Genome Sequence of Paenibacillus mucilaginosus 3016, a Bacterium
RT Functional as Microbial Fertilizer.";
RL J. Bacteriol. 194:2777-2778(2012).
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DR EMBL; CP003235; AFC33166.1; -; Genomic_DNA.
DR RefSeq; WP_013920601.1; NC_016935.1.
DR AlphaFoldDB; H6NKM9; -.
DR STRING; 1116391.PM3016_6541; -.
DR KEGG; pmq:PM3016_6541; -.
DR HOGENOM; CLU_016107_2_1_9; -.
DR Proteomes; UP000007523; 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; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 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:UP000007523}.
FT DOMAIN 44..510
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 534 AA; 58360 MW; 19A904D974474F30 CRC64;
MLDLILRNGR VIDGSGNPWF LGDVGIKDGR IAAVGRVDQE ARSVVDVHRQ VIAPGFIDGH
CHSDLMLLDH PHSEIKLSQG VTAEVVGNCG LAPAPLVPER AELLQSYVQP VLGRTDWAWP
WETLPGYMDT LARCGPSSHV ATYAAHGALR IAVMGFDNRP AAPHELERMK QLLAEGMQAG
AIGLSIGLLY APGSYTSKEE LAELCSVLPR YGGLFSTHIR GEGSSLLPSV REVIWIAEKA
GVPLHISHLK AAGRRSWGQV LEAVEEIENA RARGLDVTCD VYPYAAGSTT LTTVLPPWVL
ERGIEGALET FRDPAMRKRI REELTEEQED WDNLVCSTGW DSVVISAMHT EAGRALEGRS
IADIAAARGL PPADAMMDLL LEEEGRISIV YFHMSDDDVR EVVRYDKSLI ASDSLTCETG
KPHPRLYGTF PRLFAKYVRE ERALSLEQAV RKVTSFPVQR FKLGKRGLLV PGYAADITVF
DPETIQDRAT YQDPRQFPAG ISHVLVGGSP TLQDGAHTRA RAGSLIRAVS CCSH
//
