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Database: UniProt
Entry: S3N1A6_9GAMM
LinkDB: S3N1A6_9GAMM
Original site: S3N1A6_9GAMM 
ID   S3N1A6_9GAMM            Unreviewed;       451 AA.
AC   S3N1A6;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Dihydroorotase {ECO:0000313|EMBL:EPF73905.1};
GN   ORFNames=F945_01784 {ECO:0000313|EMBL:EPF73905.1};
OS   Acinetobacter rudis CIP 110305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF73905.1, ECO:0000313|Proteomes:UP000014568};
RN   [1] {ECO:0000313|EMBL:EPF73905.1, ECO:0000313|Proteomes:UP000014568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF73905.1,
RC   ECO:0000313|Proteomes:UP000014568};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL   Submitted (JUN-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:EPF73905.1}.
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DR   EMBL; ATGI01000022; EPF73905.1; -; Genomic_DNA.
DR   RefSeq; WP_016656191.1; NZ_KE340353.1.
DR   AlphaFoldDB; S3N1A6; -.
DR   STRING; 632955.GCA_000829675_02595; -.
DR   PATRIC; fig|421052.3.peg.1741; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_1_1_6; -.
DR   OrthoDB; 5687299at2; -.
DR   Proteomes; UP000014568; 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   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; 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   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:UP000014568}.
SQ   SEQUENCE   451 AA;  50737 MW;  3E36BCEFFAA24385 CRC64;
     MNFRQLPDLI IHNANIVNEG LCQIGDVLIQ QGRIAKIQSS ITGFYHAKSI EANGAWLIPG
     MIDDQVHFRD PGSPQKGRFS TESVAAAVGG ITSIMDMPNT QPATLDLAAL QYKKDIAAKY
     SMTNYAFHFG VSADNLNIVE NLDPKLVSGV KVFMGASTGN MLVDDVQVLE RLFANVPTIL
     LSHCESTPRI KQLEQYYRQK YGDAVPAVLH PQIRDKQACF NSSQLAVALA EKYGTQLHVL
     HISTARELCL FKNLPLDKKY ITAEVCVHHL SFDESDYAHQ GHLIKCNPAI KTLMDKQTLI
     EAVAHTDRLD IIGTDHAPHT WQEKQKSYFQ APAGLPLVQH AIPALMDLVA DRLLPIETLV
     RKTSHQVADL FRIKDRGYIR EGYWADLVLI KENHDQQAVS QQRNFMYCGW TPFQNKTFRY
     LVDTTIISGQ LAWHNQQVFL NCRGHALEID R
//
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