ID E4RQT4_LEAB4 Unreviewed; 524 AA.
AC E4RQT4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ADQ17540.1};
GN OrderedLocusNames=Lbys_1834 {ECO:0000313|EMBL:ADQ17540.1};
OS Leadbetterella byssophila (strain DSM 17132 / JCM 16389 / KACC 11308 / NBRC
OS 106382 / 4M15).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Leadbetterella.
OX NCBI_TaxID=649349 {ECO:0000313|EMBL:ADQ17540.1, ECO:0000313|Proteomes:UP000007435};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Teshima H., Brettin T., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Leadbetterella byssophila DSM 17132.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ17540.1, ECO:0000313|Proteomes:UP000007435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17132 / JCM 16389 / KACC 11308 / NBRC 106382 / 4M15
RC {ECO:0000313|Proteomes:UP000007435};
RX PubMed=21475582; DOI=10.4056/sigs.1413518;
RA Abt B., Teshima H., Lucas S., Lapidus A., Del Rio T.G., Nolan M., Tice H.,
RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K.,
RA Pati A., Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Goker M., Tindall B.J.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Leadbetterella byssophila type strain
RT (4M15).";
RL Stand. Genomic Sci. 4:2-12(2011).
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DR EMBL; CP002305; ADQ17540.1; -; Genomic_DNA.
DR RefSeq; WP_013408589.1; NC_014655.1.
DR AlphaFoldDB; E4RQT4; -.
DR STRING; 649349.Lbys_1834; -.
DR KEGG; lby:Lbys_1834; -.
DR eggNOG; COG1228; Bacteria.
DR HOGENOM; CLU_023620_4_1_10; -.
DR OrthoDB; 9797498at2; -.
DR Proteomes; UP000007435; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 2.
DR InterPro; IPR006680; Amidohydro-rel.
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; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007435};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..524
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003186863"
FT DOMAIN 380..464
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 524 AA; 59158 MW; 9C029AAE5896E7D1 CRC64;
MKRLFLLLSL ATSLCFAQVQ DAPKRTEGEG PFPQLIIRGV TLINSTGAPP LGPVDIVVKQ
NRIAEVRQVG YPGVPIDPRR RPVANPGDKE LECTGMYLMP GFVDMHGHIG GRAQGTPSEY
VFKLWLGHGI TTIREPGSGN GIDWTLNHKK KSWNNEITAP RIMAYTTFGQ GSREGIHTAE
AARNWVRENA KKGADGIKFF GAAPEVFRAA LDENKKLGLR SACHHAQLEV ARMNVLATAK
AGLTSMEHWY GLPEALFSDR TLQDYPSDYN YNNEQHRFEE AGNLWKQAAE PGSDKWYQVM
DELLKLDFTL DPTFNIYDAN RDLMRARTAE WHEEYTLPSL WRFYGPSRMS HGSYWLNWGT
KQEIKWKENY RLWMRFVNEY KNKGGRVTTG SDNGFIYQLY GFGYIRELEL LRESGFHPLE
VIQSATIKGA EALGLDKEIG SVEVGKLADF VITTENPLSN FSTLYGTGAI KVDENNEVVR
VGGVRYTVKD GIVYDAPQLL KDVRQIVKDA KEKENFEIKQ PGIK
//