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
//