ID   A0A1H6YA99_9BACT        Unreviewed;       447 AA.
AC   A0A1H6YA99;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SEJ34122.1};
GN   ORFNames=SAMN05192553_103345 {ECO:0000313|EMBL:SEJ34122.1};
OS   Cyclobacterium xiamenense.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=1297121 {ECO:0000313|EMBL:SEJ34122.1, ECO:0000313|Proteomes:UP000199403};
RN   [1] {ECO:0000313|Proteomes:UP000199403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10761 {ECO:0000313|Proteomes:UP000199403};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNZH01000003; SEJ34122.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6YA99; -.
DR   STRING; 1416801.SAMN05192553_103345; -.
DR   Proteomes; UP000199403; 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   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}.
FT   DOMAIN          51..425
FT                   /note="Amidohydrolase-related"
FT                   /evidence="ECO:0000259|Pfam:PF01979"
SQ   SEQUENCE   447 AA;  50341 MW;  203A165507C6A190 CRC64;
     MKRILIRNAN IVNEGKIMQG DLYIKEGLIF AVGGDLSGYE ADTEIDGSGK YLLPGLIDDQ
     VHFREPGLTH KAEIYTESKA AVAGGITSYM EMPNTVPQAT TLELLEEKYE LAAKKSLANY
     SFYLGATNDN IETIKKVDPQ TVCGVKVFQG SSTGNMLVDN PDSLEQIFKH SPTIIATHSE
     NDHIIKENLE KYKKEYGEDI PVRFHPKIRS WQACYDASKT VVDMARMYGS KLHVLHISTG
     EEVKLFDKDL PLAEKRITAE ACVHHLWFSE EDYERKGNLI KWNPAIKTAK DREAILKGLL
     DGHIDVLATD HAPHTLEEKS KRYQSAPSGG PLVQHCLPAL LEMYHKGLIS LEQIVQKSSH
     NVAILFEIEK RGYLRPGYHA DMVLVDLHDP WEVSRDNVLS KCGWSPFEGQ TFRSKITHTI
     VSGHLAYANG TFHEERQGQR LKFSRNV
//