ID A0A0Q7Z417_9SPHN Unreviewed; 579 AA.
AC A0A0Q7Z417;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQZ65105.1};
GN ORFNames=ASD67_06540 {ECO:0000313|EMBL:KQZ65105.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ65105.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ65105.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ65105.1,
RC ECO:0000313|Proteomes:UP000051141};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ65105.1}.
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DR EMBL; LMGF01000003; KQZ65105.1; -; Genomic_DNA.
DR RefSeq; WP_056344979.1; NZ_LMGF01000003.1.
DR AlphaFoldDB; A0A0Q7Z417; -.
DR Proteomes; UP000051141; Unassembled WGS sequence.
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 Hydrolase {ECO:0000313|EMBL:KQZ65105.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..579
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006331639"
FT DOMAIN 76..567
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 579 AA; 60892 MW; 3AD702E5EEA4FDE5 CRC64;
MSKPAVSAAL ALALALSAGT AAARDKAPAD LILTNARVYT VEDKQPWAEA VAIRDGKIVA
VGSIAAVGKL RGAATRTVDL GGKLVLPAFG DAHVHPLFGA LSRSRCPLQD GKTIADYQAL
IAKCVAAVPG DGAIYGIGWS DALFPPSGIP NKALLDAVST TRPLIFESTG GHTYWLNSKA
LAVAGITRDT KDPANGTIDR DPATGEPVGS LQEAAMDLVK HMIPPPSAAE IQNSILYVAD
HFNSLGIVSW NDAGVEYDAD GGSAMVDAYK AVLDAGKLTS HVAVSLKWKN EQGMEQLPGL
LRAAERANRL GISTHTVKFY VDGVIPQKTA FMLAPYENSG DERGKPQIAP DLLKQAVTAV
DGKGMHAFLH AIGDGGVHIS LDAIEAARKA NGARPTHHMI THMNVVDPAD QPRFGKLSTF
AQFQPTWASW YDYMELTVAA IGPKRATYIY PAGSIVRAGG KLAYGADWPV GGANPLEGIE
VAMTRRTAGD PNAKPLLPDE GVSLKEAIAS HTINVAYVNG FDAVTGSIKT GKSADLVVLD
KDIFNLPAYE ISKTKVLVTL FEGKPVFGDW TDAASPAAR
//
