GenomeNet

Database: UniProt
Entry: A0A0N9N827_9ACTN
LinkDB: A0A0N9N827_9ACTN
Original site: A0A0N9N827_9ACTN 
ID   A0A0N9N827_9ACTN        Unreviewed;       392 AA.
AC   A0A0N9N827;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:ALG84235.1};
GN   ORFNames=ACH46_06580 {ECO:0000313|EMBL:ALG84235.1};
OS   Gordonia phthalatica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG84235.1, ECO:0000313|Proteomes:UP000063789};
RN   [1] {ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA   Jin D., Kong X., Bai Z.;
RT   "Complete genome sequence and metabolic analysis of phthalate degradation
RT   pathway in Gordonia sp. QH-11.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALG84235.1, ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|EMBL:ALG84235.1,
RC   ECO:0000313|Proteomes:UP000063789};
RX   PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA   Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT   "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT   isolated from activated sludge.";
RL   Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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; CP011853; ALG84235.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N9N827; -.
DR   STRING; 1136941.ACH46_06580; -.
DR   KEGG; goq:ACH46_06580; -.
DR   PATRIC; fig|1136941.3.peg.1347; -.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000063789; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ALG84235.1}.
FT   DOMAIN          190..283
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   392 AA;  41008 MW;  F787D0C3365F9E0B CRC64;
     MSSPVIDAWL AANLGRVVGW RREIHAEPEL SMAEFQTTAK VVQILTDAGL RPKVLPKGTG
     VVCDFGPTDK PRIGLRADLD GLPIPEQTGL PFTSKVENVS HSCGHDAHAA ILLGTGLLLA
     DHLAAGNELP FGVRLLFQAA EEVMPGGALD AIDAGATDGL TRIFALHCDP HLAAGTVGLH
     VGALTSAADR VEVHFRGPGG HTSRPHLTAD LVYAMGTVIT GLPGFLSRRV DPRSGTVMVF
     GAAHSGDASN AIPQEGRLRG TVRTGDRAVW QDLEPLVRNI VGELVAPLGV NYDLTYVRGV
     PPVVNDGDSV AMLRRSVDLI GPGAAVETPQ SPGGEDFAWY LESVPGAMAR LGVWSGVGPH
     CDLHQPNFDI DERALGVGVA TLAGVILGGE LQ
//
DBGET integrated database retrieval system