ID A0A120G9H2_9SPHN Unreviewed; 547 AA.
AC A0A120G9H2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Metal-dependent hydrolase {ECO:0000313|EMBL:KWV90388.1};
GN ORFNames=AUC45_14050 {ECO:0000313|EMBL:KWV90388.1};
OS Erythrobacter sp. YT30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV90388.1, ECO:0000313|Proteomes:UP000055668};
RN [1] {ECO:0000313|EMBL:KWV90388.1, ECO:0000313|Proteomes:UP000055668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YT30 {ECO:0000313|EMBL:KWV90388.1,
RC ECO:0000313|Proteomes:UP000055668};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. YT30.";
RL Submitted (OCT-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:KWV90388.1}.
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DR EMBL; LMAF01000003; KWV90388.1; -; Genomic_DNA.
DR RefSeq; WP_067604085.1; NZ_LMAF01000003.1.
DR AlphaFoldDB; A0A120G9H2; -.
DR STRING; 1735012.AUC45_14050; -.
DR OrthoDB; 9811399at2; -.
DR Proteomes; UP000055668; 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:KWV90388.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055668};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..547
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007165949"
FT DOMAIN 71..546
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 547 AA; 59164 MW; C94C7DE7277DCCC0 CRC64;
MQFLTRAALC ALALSVSFPA LADTLVDNVD GITVDDAGEI KRFTGIVFDD EGRITQVLER
GDDRPSTDFA VDGDGRVMLP GMIDAHVHVM DIGFAALTLD LSDTTSLEGA LAKIKQFAEE
NPGRPWILGR GWNQEKWGLG RFPTAAELDS VVSDRPVWLE RADNHANWAN TVAMDRAGIS
AATMDPEGGK VIRDASGNPS GVFVDNAIAL VGDSVPKPRP ADRDAAFTKA QEVLLTNGIT
AVADMGTPME DWQTFRRAGD LGTLNIRIMS YADSIEAMEL IGGPGPTPWL YDDKLRLVGV
KLYLDGALGS RGAVLKEPYS DAPNTRGLPL LTPAQLRNRM SRAALDNFQT AIHAIGDAAN
ADVLFAIEEL NETYKGDRRW RIEHAQIVDP ADLQKFGEYG IIASMQPLHQ TSDREMAEAR
LGPNRLGGAY AWRSVLEAGG QLAFGSDAPV EPADAFAGIA VAISRVDENG EPFGGWRAEE
TVSREDALRA FTADAAFAGF AEGRFGRLIV GERADFLLVD RDPFLSSPGE IRETEIEQVW
VGGNRVR
//
