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Database: UniProt
Entry: A0A1H1NG78_9CELL
LinkDB: A0A1H1NG78_9CELL
Original site: A0A1H1NG78_9CELL 
ID   A0A1H1NG78_9CELL        Unreviewed;       536 AA.
AC   A0A1H1NG78;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Amidohydrolase 3 domain-containing protein {ECO:0000259|Pfam:PF07969};
GN   ORFNames=SAMN04489860_0526 {ECO:0000313|EMBL:SDR97993.1};
OS   Paraoerskovia marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Paraoerskovia.
OX   NCBI_TaxID=545619 {ECO:0000313|EMBL:SDR97993.1, ECO:0000313|Proteomes:UP000185663};
RN   [1] {ECO:0000313|EMBL:SDR97993.1, ECO:0000313|Proteomes:UP000185663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22126 {ECO:0000313|EMBL:SDR97993.1,
RC   ECO:0000313|Proteomes:UP000185663};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT629776; SDR97993.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1NG78; -.
DR   STRING; 545619.SAMN04489860_0526; -.
DR   eggNOG; COG1574; Bacteria.
DR   Proteomes; UP000185663; Chromosome i.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 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; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642:SF25; EXOENZYMES REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 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:UP000185663}.
FT   DOMAIN          51..534
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   536 AA;  57639 MW;  87F1A501252F7072 CRC64;
     MGAPELILIN ASVVTVDDAG STAEAVAVAD GKIVAVGTTD EIRALADEST EVLDLAGKTV
     VPGFIDPHSH ITAGAPYIKH AALHTPPVGD TRTVQDILRK LGEARDRNNA QPGDWILGWG
     YYPDEMDDGG KITAAIIDEE FSDYRVALIH ISNHGAVVNG KVLELLEYTA ETPDPDGGTI
     IRTEGSQDPS GEIWEQAFFP LMFQLPPAGE EELRAMAAEY ARWGYTVAQD GAADMSAVNL
     VRESATANPL PIDVKSLVFF PDLQKAIDAK IIGTEVGGHS VHGTKLILDG SPQGRTANVT
     EEYVTGGPSG ETHWHGIAVI DQDETNSLVE LAYRNGVQVF AHCNGDASVD QLLTAHRAAV
     EAGAEAPGRT VPIHSQVMRL DQLDDYVAED FEPSMFTIHT WIFGDTHVKN FGEERAFGIS
     PMRSAIDKGL HPTNHSDFPV TPMNPLQLMW TAVVRRSTGG TVIGEAQRIT PLEALQALTI
     NAAYEYREEA VRGSIEIGKK ADFAVLDANP IEADADAIKD IAVVRTIKDG RTVFEA
//
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