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Entry: A0A212S120_9PROT
LinkDB: A0A212S120_9PROT
Original site: A0A212S120_9PROT 
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
//
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