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Database: UniProt
Entry: A0A0A8UXT9_LEGHA
LinkDB: A0A0A8UXT9_LEGHA
Original site: A0A0A8UXT9_LEGHA 
ID   A0A0A8UXT9_LEGHA        Unreviewed;       567 AA.
AC   A0A0A8UXT9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Putative amidohydrolase {ECO:0000313|EMBL:CEK11957.1};
GN   ORFNames=LHA_2965 {ECO:0000313|EMBL:CEK11957.1};
OS   Legionella hackeliae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=449 {ECO:0000313|EMBL:CEK11957.1, ECO:0000313|Proteomes:UP000032803};
RN   [1] {ECO:0000313|Proteomes:UP000032803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC35250 {ECO:0000313|Proteomes:UP000032803};
RA   Gomez-Valero L.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LN681225; CEK11957.1; -; Genomic_DNA.
DR   RefSeq; WP_045107052.1; NZ_UGOC01000002.1.
DR   AlphaFoldDB; A0A0A8UXT9; -.
DR   STRING; 449.LHA_2965; -.
DR   KEGG; lha:LHA_2965; -.
DR   PATRIC; fig|449.7.peg.1502; -.
DR   HOGENOM; CLU_009942_2_0_6; -.
DR   OrthoDB; 5734927at2; -.
DR   Proteomes; UP000032803; Chromosome I.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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   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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CEK11957.1}.
FT   DOMAIN          83..560
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   567 AA;  63039 MW;  0A37423ECE417744 CRC64;
     MKRPTVFLIS IGLAILFFSL SCHSQKEAPL FCQNATIIYT NATFITLDPK QPVASAVAVS
     KQRLLAVGNS ASLIKNCRGQ DTQVIDLQGA FVVPGFIDTY SKFLLYGWLS QNAVDFSTTN
     IFQRPDWREI KTIDAFLNAL KNKTPNAAGW LIVNGYDPVR ITGSALNQTM LNNLQSNTPT
     LVLYASGNQA LLNQAAIQKL ATFDNNTQIA VDNNGFIRDT ALITLLTKLI NKEDIPKVIQ
     QAVHQYTEQG YTTVTETMFN PTWISAYEQL TLQPEFAVDV ILMPSTIAEK KRMDLTYQDL
     PRLYVGPVLF KVDGAAQDDA AFLTRPVLQP NLHSNNRWPE SLTKSPRELE QLLKTADREK
     IPVALECNGD AAIDLALNII NKMRNLPNEQ PFNAVIINAP FVRSDQLQRM RQLNVKVSWF
     APHFYYWGAA LCNIFRDAEG NYYTNPLANT KKIMTTLSVQ ANSPTTPPVP LQMIKFINTG
     ELQNWQPNNP KCSPKPPAKS SVNITDAIKA LTLDAAVLYG LENDKGSLVP GKLADMTILN
     ENPLKSNLQN IHVLGTISRG VLHLNNH
//
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