ID Q01XP4_SOLUE Unreviewed; 465 AA.
AC Q01XP4;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:ABJ85571.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:ABJ85571.1};
DE Flags: Precursor;
GN OrderedLocusNames=Acid_4612 {ECO:0000313|EMBL:ABJ85571.1};
OS Solibacter usitatus (strain Ellin6076).
OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae;
OC Solibacter.
OX NCBI_TaxID=234267 {ECO:0000313|EMBL:ABJ85571.1};
RN [1] {ECO:0000313|EMBL:ABJ85571.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ellin6076 {ECO:0000313|EMBL:ABJ85571.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Janssen P.H., Kuske C.R., Richardson P.;
RT "Complete sequence of Solibacter usitatus Ellin6076.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000473; ABJ85571.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01XP4; -.
DR STRING; 234267.Acid_4612; -.
DR KEGG; sus:Acid_4612; -.
DR eggNOG; COG3653; Bacteria.
DR HOGENOM; CLU_016107_3_0_0; -.
DR InParanoid; Q01XP4; -.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 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; IPR023100; D-aminoacylase_insert_dom_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF07969; Amidohydro_3; 2.
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:ABJ85571.1}.
FT DOMAIN 61..116
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
FT DOMAIN 184..448
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 465 AA; 49594 MW; 7412E7D94FEBEA24 CRC64;
MIRAALLVLM ALPMYGQTYD LVIANGRVLD PASNLDAVRH IGIRGGKIAA VSTTPLGGRA
TIDATGLVVA PGFIDLHSHG QTPENYRFKA RDGVTTALEL EVGANPVAAW YAEREGRALI
NFGATSGELP ARIAVMHDTG KLLPRDKAVE RAATAEEFTN VLTRVGRGID EGALGIGMGI
AYLPHETRAE VLELFRLAAQ RKVPVYIHMR NGGPLEPGVI DALQEVIADA AASGASVHVV
HITSMGLREA PLCLAMIQGA RARGLDITTE AYPYTAGMTD LGSAIFDEGW QQRQGGIGFG
DLQWAATGER LTAESFAKYR QQGGFVAIHS IPENIVQLAM ANPLVMIASD GILEEGKGHP
RAAGTYARVL GRYVRELKSL TLMEAVRKMT QMPADRLGMP AKGRIANGVD ADLTIFDAAH
VTDRATFESP ARYSEGIPYV IVGGTVVVNR GELVPNVTPG HAVRR
//
