ID   A0A095AZK6_9SPHN        Unreviewed;       599 AA.
AC   A0A095AZK6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KGB55970.1};
GN   ORFNames=FG91_00854 {ECO:0000313|EMBL:KGB55970.1};
OS   Sphingopyxis sp. LC81.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1502850 {ECO:0000313|EMBL:KGB55970.1, ECO:0000313|Proteomes:UP000029574};
RN   [1] {ECO:0000313|EMBL:KGB55970.1, ECO:0000313|Proteomes:UP000029574}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC81 {ECO:0000313|EMBL:KGB55970.1,
RC   ECO:0000313|Proteomes:UP000029574};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGB55970.1}.
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DR   EMBL; JNFD01000007; KGB55970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A095AZK6; -.
DR   STRING; 1502850.FG91_00854; -.
DR   PATRIC; fig|1502850.3.peg.868; -.
DR   eggNOG; COG1228; Bacteria.
DR   Proteomes; UP000029574; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 1.20.58.520; Amidohydrolase; 1.
DR   Gene3D; 3.30.110.90; Amidohydrolase; 1.
DR   Gene3D; 3.40.50.10910; Amidohydrolase; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   PANTHER; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KGB55970.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..599
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001912889"
FT   DOMAIN          84..410
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   599 AA;  63067 MW;  D11F186995E00208 CRC64;
     MASFRKMLVA GTAIAAGLGW ASQSVLAEPG GDVVAITGAT IFDATGKEPY RGTVVVRGGR
     IEAVGADVRV PKGAKIVRAD GKALLPGFID VHTHWSPSGS PGALPQIANA YLASGVTTVN
     DFHQQPEAFA PRRAWLADIY APHVNFVARM STPGGHGADW ADTNTTKWVA TAESARREVQ
     ALQVYRPDYV KAFADGWRYG QLPEETSMNV ETLAALADEA HKHGQRVLTH TVTVERGKIA
     ADAGVDVIAH SIQDGVLDAA AIARIKKAGT FYAPTLAIYQ LKPDEMGPGR KDDAATRQRI
     RKYGFAEENV RNLFAAGVTI AVGTDAGIGG AKHGVSTLQE MELLVAAGLT PKAALLAGTS
     NSALALGLSS DRGTIEKGKR ADLVLIDGKP WEAIGDVNKI DRVFVDGKLV HGGGVKLPAG
     NLANALSASP AAALIDDFER ADGRSSLDTL RLTDMDGGVE RSSVVTNRVT HSGGNGSALA
     FAVQMSLKDK PEGGVLVPLS RGSVRPVDAR KFEGVRLDMR GAGRYLLVVN TLAGEFTAPI
     EAKEGWSELR IPFAALVPTR PGRGDPPSWR GDDLVQVGVV VQREAGASAW GEMDNLGFY
//