ID   M7XTN4_9BACT            Unreviewed;       451 AA.
AC   M7XTN4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:EMS31837.1};
GN   ORFNames=C943_01796 {ECO:0000313|EMBL:EMS31837.1};
OS   Mariniradius saccharolyticus AK6.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Mariniradius.
OX   NCBI_TaxID=1239962 {ECO:0000313|EMBL:EMS31837.1, ECO:0000313|Proteomes:UP000010953};
RN   [1] {ECO:0000313|EMBL:EMS31837.1, ECO:0000313|Proteomes:UP000010953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK6 {ECO:0000313|EMBL:EMS31837.1,
RC   ECO:0000313|Proteomes:UP000010953};
RA   Vaidya B., Khatri I., Tanuku N.R.S., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Mariniradius saccharolyticus AK6.";
RL   Submitted (JAN-2013) 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:EMS31837.1}.
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; AMZY02000017; EMS31837.1; -; Genomic_DNA.
DR   RefSeq; WP_008630051.1; NZ_AMZY02000017.1.
DR   AlphaFoldDB; M7XTN4; -.
DR   STRING; 1239962.C943_01796; -.
DR   eggNOG; COG0044; Bacteria.
DR   InParanoid; M7XTN4; -.
DR   OrthoDB; 9765462at2; -.
DR   Proteomes; UP000010953; Unassembled WGS sequence.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd01318; DHOase_IIb; 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; 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:SF4; 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; 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:UP000010953}.
FT   DOMAIN          53..427
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   451 AA;  50165 MW;  3BA982F6EF18A99E CRC64;
     MKKKSILITG ANIVNEGRIR PSDVLIKDGF IERIDANLSS ISADILIDGS GKYLFPGLID
     DQVHFREPGL THKADIYTES KSAVAGGVTS YMEMPNTVPP ATTIALLEQK FRIASEKSLA
     NYSFFFGASN DNIAEILQVD PQNVCGVKVF QGSSTGNMLV DNPESLERIF AECKVLIATH
     SENDEIIKTN LEKYKSEFGD NIPVKYHPLI RSEEACYDAS KKVVALAKKY GSKLHILHIS
     TAREVGLFDN SLPLEQKRIT AEACIHHLWF CDEDYESKGN FIKWNPAVKT KNDRSTILQG
     VLDGRIDVIA TDHAPHTREE KSKAYSSAPS GGPLVQHSLV ALLDMYHQGK ISLEMIAQKA
     AHNVAILFEI DKRGFIREGF YADLVLVDLN SPWTVTPDNI LSKCGWSPFE GHTFRSKVTH
     TIVSGHLAYE NGTFHEEQKG VRLKFSRKIN S
//