ID A0A212S120_9PROT Unreviewed; 440 AA.
AC A0A212S120;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:SNB78661.1};
GN ORFNames=SAMN07250955_11917 {ECO:0000313|EMBL:SNB78661.1};
OS Arboricoccus pini.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Arboricoccus.
OX NCBI_TaxID=1963835 {ECO:0000313|EMBL:SNB78661.1, ECO:0000313|Proteomes:UP000197065};
RN [1] {ECO:0000313|EMBL:SNB78661.1, ECO:0000313|Proteomes:UP000197065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B29T1 {ECO:0000313|EMBL:SNB78661.1,
RC ECO:0000313|Proteomes:UP000197065};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FYEH01000019; SNB78661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212S120; -.
DR OrthoDB; 9775759at2; -.
DR Proteomes; UP000197065; 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 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 InterPro; IPR011612; Urease_alpha_N_dom.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF4; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 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:UP000197065}.
FT DOMAIN 3..36
FT /note="Urease alpha-subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00449"
FT DOMAIN 53..421
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 440 AA; 48121 MW; F1CEF524F146E9BB CRC64;
MTAYDLVLAN GQLVRPWGIE QADIGVRDGH IVAIGDLRTA VTAERIDCAG LHVLPGLIDP
HVHLRDPGDP AIESIPDGTK GAVLGGLTAV FDMPNTAESV INNLRLTRKR DGIKGRSWCD
IGFYVGATKT NIAELAALEE EPGVCAVKVF AGSSTGDLLV EDDESLRRVM LNGRRRICYH
SEDEERLQAR KPLFAEGGPY RLHMEWRDVE CAYLGTRRLM ALARETGRPA HILHVSTAEE
LAYLRDFRDV ASVELLVNHL TQSAPEAYER LGGYAVMNPP IREQRHVDAA WAAVADGMVD
TIGSDHAPHP KAAKERPWPA TASGLTGVQT LVPMMLDQVS QGRLSLTRLV DLMAAGPARI
YGAVAKGRLA AGYDADFTIV DMGRKRTITN DWIVSPCGWT PFDGQTCQGW PVMTIVRGQL
VMREDELLGK PIGQPVRFRS
//