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Database: UniProt
Entry: E4PQU0_MARAH
LinkDB: E4PQU0_MARAH
Original site: E4PQU0_MARAH 
ID   E4PQU0_MARAH            Unreviewed;       582 AA.
AC   E4PQU0;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=N-acyl-D-glutamate amidohydrolase {ECO:0000313|EMBL:ADP97890.1};
GN   OrderedLocusNames=HP15_2126 {ECO:0000313|EMBL:ADP97890.1};
OS   Marinobacter adhaerens (strain DSM 23420 / HP15).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP97890.1, ECO:0000313|Proteomes:UP000007077};
RN   [1] {ECO:0000313|EMBL:ADP97890.1, ECO:0000313|Proteomes:UP000007077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX   PubMed=21304739;
RA   Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA   Glockner F.O., Grossart H.P., Ullrich M.S.;
RT   "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT   diatom-interacting marine microorganism.";
RL   Stand. Genomic Sci. 3:97-107(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA   Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA   Gloeckner F.O., Ullrich M.S.;
RT   "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001978; ADP97890.1; -; Genomic_DNA.
DR   RefSeq; WP_014577468.1; NC_017506.1.
DR   AlphaFoldDB; E4PQU0; -.
DR   STRING; 225937.HP15_2126; -.
DR   KEGG; mad:HP15_2126; -.
DR   PATRIC; fig|225937.3.peg.2141; -.
DR   eggNOG; COG3653; Bacteria.
DR   HOGENOM; CLU_016107_1_0_6; -.
DR   Proteomes; UP000007077; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR013108; Amidohydro_3.
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   Hydrolase {ECO:0000313|EMBL:ADP97890.1}.
FT   DOMAIN          48..201
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   582 AA;  65264 MW;  30102A3BF314D436 CRC64;
     MNQFDTLIVG GRYFDGTGGP SRIAHVGIKD GRVAEVFDQQ PEPGLATRTI DASGCWVTPG
     FLDTHTHYDA ELLVAPSLSE SVRHGVTTVL IGSCSLSMVC SDPEDASDIF TRVETVPREK
     VLPILKQHKS WQTPKEWVAF MDQHPLGPNV ISFLGHSDLR TAVMGLHRAT DRNVTPTPEE
     QQKMEALLEE ALQEGFLGLS TMCLKWDKVD GDREWSKSLP STYARWREVS RLNALLRRYG
     RVHQGAPNAA NPLQVTQYLK ETLGWLRKPL KTTLIAMIDL KGNPTVKPMA SLVGWLANSF
     GGNFRWQLLP TPFTVYADGM DIVLFEEFGA GEMALDIRDQ LERNDLLKDE QYRRKFRKFY
     KEKLSPRVWQ RDFGDAVILD CPDKSVVGRN FAELAADRGI HVVDFFLDMV VAHGRSLRWF
     TTVGNHRKDR LRKMVTNPGA LITFSDAGAH IRNMAFYNLP LRFLKLVNES HGEGEPIMSL
     ERAVHRLTGE QADWLGVDAG HIRVGDRADI TVLDPRGLDQ DLEQVEWGEM ENFGLERMVN
     RVPGCVREVL INGRPAVTNG EVQPALGRES GYGHFLRAGA SG
//
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