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Database: UniProt
Entry: R6I508_9FIRM
LinkDB: R6I508_9FIRM
Original site: R6I508_9FIRM 
ID   R6I508_9FIRM            Unreviewed;       401 AA.
AC   R6I508;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:CDB41544.1};
GN   ORFNames=BN517_01611 {ECO:0000313|EMBL:CDB41544.1};
OS   Ruminococcus sp. CAG:177.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262952 {ECO:0000313|EMBL:CDB41544.1, ECO:0000313|Proteomes:UP000018315};
RN   [1] {ECO:0000313|EMBL:CDB41544.1, ECO:0000313|Proteomes:UP000018315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:177 {ECO:0000313|Proteomes:UP000018315};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC       to dihydroorotate. {ECO:0000256|ARBA:ARBA00002368}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       DHOase family. Class I DHOase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010286}.
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:CDB41544.1}.
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DR   EMBL; CBDQ010000045; CDB41544.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6I508; -.
DR   STRING; 1262952.BN517_01611; -.
DR   Proteomes; UP000018315; Unassembled WGS sequence.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01317; DHOase_IIa; 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; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR00857; pyrC_multi; 1.
DR   PANTHER; PTHR43668; ALLANTOINASE; 1.
DR   PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018315}.
FT   DOMAIN          33..346
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   401 AA;  44289 MW;  A8954BDCF46B73B1 CRC64;
     MTHDFACRYE KIRAFAEKFL ADGGLLSAVE NYIIVPGLCD VHVHFREPGF SYKETIASGS
     AAAAHGGYTA VCTMPNLDPV PDSAEHLQVQ LDAIKRGAAI KVLPYGAITV GEKGEKLADM
     EAMSDKVCAF SDDGKGVQND EMMREAMTAA KRLGKIIAAH CEDNSLLFDG YIHDGEYARM
     HGHRGISSAS EYKQIERDLR LAEETGCAYH ICHISTKESV ELIRQAKARG VNVTCETAPH
     YLVLCDEDMQ EDGRFKMNPP LRSREDKQAL IEGIKDGTID MIATDHAPHS AEEKGRGLEK
     SLMGVVGLET AFPVLYTELV TKNIITLDRL VELMSFKPKE RFGIDTNNDF AVFDISEAYK
     IDPEDFLSMG RATPFAGREV FGRCLLTVHN GKVVYKAEDR A
//
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