ID A0A0R0C5Q5_9GAMM Unreviewed; 448 AA.
AC A0A0R0C5Q5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:KRG65053.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:KRG65053.1};
GN ORFNames=ABB26_04305 {ECO:0000313|EMBL:KRG65053.1};
OS Stenotrophomonas humi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG65053.1, ECO:0000313|Proteomes:UP000050864};
RN [1] {ECO:0000313|EMBL:KRG65053.1, ECO:0000313|Proteomes:UP000050864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG65053.1,
RC ECO:0000313|Proteomes:UP000050864};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:KRG65053.1}.
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DR EMBL; LDJI01000009; KRG65053.1; -; Genomic_DNA.
DR RefSeq; WP_057632358.1; NZ_LDJI01000009.1.
DR AlphaFoldDB; A0A0R0C5Q5; -.
DR STRING; 405444.ABB26_04305; -.
DR PATRIC; fig|405444.3.peg.3575; -.
DR OrthoDB; 5687299at2; -.
DR Proteomes; UP000050864; Unassembled WGS sequence.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KRG65053.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 52..429
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 448 AA; 49302 MW; 9D1121B95AE286F9 CRC64;
MSSTLITNAR MVNEGRTFDG DLRIENGRIA QIGTGLTPRD GEQVVDAAGR WLLPGMIDDQ
VHFREPGLTH KGDIASESAA AVAGGLTSFM DMPNTNPPTL DSTILEAKYE LAKGRAWANY
GFYHGASNDN LEAIRALDPK KAPGVKVFMG ASTGNMLVDN PETLDAIFRE CPTPIITHCE
DTPMIDANLK AFQEKYGDAL TPEMHPDIRS REACIKSTRL AMSLARKHGT RLHVLHISTA
DELALFEKGP LIRADGSRKQ ITAETCVHFL HFARPDYATK GNLIKCNPAI KDVADREAIT
AALADDVLDV LATDHAPHTW EEKQKPYAQA PSGLPLVQYA LVAALERVHE GKLTREQVVQ
KFAHAPAQLF DVEERGFLRE GYFADLVLVE DVPFTVKRED VLSKCGWSPF EGTTFRSRIA
STWVNGQLVW DGNKLVGAPA GQRMTYDR
//
