ID A0A0Q7SPQ5_9CAUL Unreviewed; 552 AA.
AC A0A0Q7SPQ5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQY85882.1};
GN ORFNames=ASD25_23340 {ECO:0000313|EMBL:KQY85882.1};
OS Brevundimonas sp. Root1423.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY85882.1, ECO:0000313|Proteomes:UP000051815};
RN [1] {ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY85882.1, ECO:0000313|Proteomes:UP000051815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1423 {ECO:0000313|EMBL:KQY85882.1,
RC ECO:0000313|Proteomes:UP000051815};
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:KQY85882.1}.
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DR EMBL; LMFL01000020; KQY85882.1; -; Genomic_DNA.
DR RefSeq; WP_056617387.1; NZ_LMFL01000020.1.
DR AlphaFoldDB; A0A0Q7SPQ5; -.
DR Proteomes; UP000051815; 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; IMIDAZOLONEPROPIONASE; 1.
DR PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 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:KQY85882.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051815};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..552
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006323013"
FT DOMAIN 68..549
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 552 AA; 58313 MW; 12BB3BEA8B84D9A4 CRC64;
MIRTLALTLL LAGAAASAEA QDMLIKGGPI YTGVDAAPTA EAVLVRDGRI AWVGKLADQP
AVPTEIPTID LKGAALFPGF TDGHAHLDGI GWRELTLNLE GSVSLADAMA RLTAWAAAHP
EGPIAGRGWI ETRWPEARFL TAADLDAAAP GRVVLLGRAD GHAVVASTPA LAAAGIDAST
VAPAGGEILK GPDGKPTGLL VDAADQLVTS LTPQADPAAL REAYRAGFRV EASYGWTGVH
FMSAPWEDIP LLEDMAADGE APLRIYNSIT PEGAAELIAG GPRSVADGRI ITRAIKYYAD
GALGSRGAAL FEPYADRPDT TGLMQITEQE IVPLYQAALK GGIQIATHAI GDRGNASVAE
WYQQALAGVA PSERPNGADV RWRIEHAQIL RPTDYHWFRD LPIIASMQPS HAIGDLYFAP
ARLGDARLDG AYAWRSLVDL GVIVVGGSDA PVERGAPLIE FYAAVARADL EGHQGPDWRP
NEAVDRATAL KMFTLWPAWA SFREAELGTI EVGKRADLTA FNVDLMTAPV ADIPKGHATL
TVVDGVVVYR KD
//