ID D9QLR8_BRESC Unreviewed; 555 AA.
AC D9QLR8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Amidohydrolase 3 {ECO:0000313|EMBL:ADL00002.1};
GN OrderedLocusNames=Bresu_0687 {ECO:0000313|EMBL:ADL00002.1};
OS Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=633149 {ECO:0000313|EMBL:ADL00002.1, ECO:0000313|Proteomes:UP000002696};
RN [1] {ECO:0000313|Proteomes:UP000002696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC {ECO:0000313|Proteomes:UP000002696};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002102; ADL00002.1; -; Genomic_DNA.
DR RefSeq; WP_013268105.1; NC_014375.1.
DR AlphaFoldDB; D9QLR8; -.
DR STRING; 633149.Bresu_0687; -.
DR KEGG; bsb:Bresu_0687; -.
DR eggNOG; COG1574; Bacteria.
DR HOGENOM; CLU_009942_1_0_5; -.
DR InParanoid; D9QLR8; -.
DR OrthoDB; 9811399at2; -.
DR BioCyc; BSUB633149:G1GM8-689-MONOMER; -.
DR Proteomes; UP000002696; Chromosome.
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:ADL00002.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002696};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..555
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003126978"
FT DOMAIN 67..552
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 555 AA; 59198 MW; 27189ED7061892CF CRC64;
MLRVFLTTAA FAALALPANA QDLVIRGGTI HTGVEAAPTA EVVIARGGRI AYAGSAADAP
PAEGLPVIDL KGATLFPGFT DGHAHLDGIG WRELTLNLEG STSVVDAMAR LTAWAETHPE
GVIVGRGWIE TRWPESANGA RFLTAADLDA AAPGRIVLLQ RADGHASVAS TPSLERLGIT
AQTEAPFGGE ILKGPDGRPT GLFVDAAEQL LAPLMPQADP EQTREAYRAG FRVEAAYGWT
GVHFMSAPWR DIPLLEAMAE AGEAPLRIYN SVTPDGAQAL FASGPRQTAD GRIITRAVKY
YADGALGSRG AALFAPYSDA PETTGLMQIT SDQIVPLYEQ ALRSGIQIAT HAIGDRGNAS
VAEWYAAALN AVPAAERPDG ADVRLRIEHA QILRPSDYHW FKDLPIIASM QPSHAIGDFH
FAPARLGDAR LDGAYAWHSL VDLGVIVVGG SDAPVERGDP LIEFYAAVAR RDLEGVQRPD
WRPDEAVDRA TALKMFTLWP AYASFRENEL GTIEVGKRAD FTAFDIDLMT VPEADIPKGH
AVLTVVDGRV VYQAD
//
