ID A0A1Y0H3D3_9BACT Unreviewed; 443 AA.
AC A0A1Y0H3D3;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:ARU42550.1};
GN ORFNames=CCB80_05600 {ECO:0000313|EMBL:ARU42550.1};
OS Armatimonadetes bacterium Uphvl-Ar1.
OC Bacteria; Armatimonadota.
OX NCBI_TaxID=2004467 {ECO:0000313|EMBL:ARU42550.1, ECO:0000313|Proteomes:UP000196284};
RN [1] {ECO:0000313|EMBL:ARU42550.1, ECO:0000313|Proteomes:UP000196284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uphvl-Ar1 {ECO:0000313|EMBL:ARU42550.1,
RC ECO:0000313|Proteomes:UP000196284};
RA Woodhouse J.N., Makower A.K., Ionescu D., Grossart H.-P., Neilan B.A.,
RA Dittmann E.;
RT "Draft genome sequences of three Uncultured Armatimonadetes, binned from a
RT Microcystis sp. enrichment culture and from Microcystis bloom
RT metagenomes.";
RL Submitted (MAY-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; CP021423; ARU42550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0H3D3; -.
DR OrthoDB; 9775759at2; -.
DR Proteomes; UP000196284; Chromosome.
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 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 InterPro; IPR011612; Urease_alpha_N_dom.
DR NCBIfam; TIGR00857; pyrC_multi; 1.
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; 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:UP000196284}.
FT DOMAIN 3..36
FT /note="Urease alpha-subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00449"
FT DOMAIN 53..423
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 443 AA; 48486 MW; 2D8DDA5672AED303 CRC64;
MQQFDLVIRG GQIVSSSGIS QADIGIRDGR IVAMGSLESS SGKTSVDVSG SHIFPGAIDT
QVHFREPGLE HKEDISTGTH AAICGGVTTI FEMPNTQPTT TSQEALADKL ARSTARAYCD
FAYFMGAAST NLEHLAEFEM LPGSPGIKMF AGSSTGDLLV EGEGDQRKVM QNGTRPMSIH
SEDEARLRHL KESLGENPHV RQHPEVRDAE AARLCTDRMI RLCEETGRPI HILHISTKEE
LPLLADAKKR GLPVTCEATP HHLTLNSDQY ETLGTLIQMN PPVRSEDHRL ALWNAVKEGL
FDVFGSDHAP HTLEEKAKPY PNSPSGMPGV QTLFPVMLDW ALKGELPLTQ LVKMLMERPA
ELFGIAGKGH IQAGYDADLA IVDLERTWTV TNEAMKSKCG WTPYAGRELK GAIEHVFLRG
EQVVQGGISL EKPIGQPVKF TWK
//
