ID E0SQF0_IGNAA Unreviewed; 409 AA.
AC E0SQF0;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Dihydroorotase, multifunctional complex type {ECO:0000313|EMBL:ADM28206.1};
GN OrderedLocusNames=Igag_1403 {ECO:0000313|EMBL:ADM28206.1};
OS Ignisphaera aggregans (strain DSM 17230 / JCM 13409 / AQ1.S1).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignisphaera.
OX NCBI_TaxID=583356 {ECO:0000313|EMBL:ADM28206.1, ECO:0000313|Proteomes:UP000001304};
RN [1] {ECO:0000313|EMBL:ADM28206.1, ECO:0000313|Proteomes:UP000001304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17230 / JCM 13409 / AQ1.S1
RC {ECO:0000313|Proteomes:UP000001304};
RX PubMed=21304693; DOI=10.4056/sigs.1072907;
RA Goker M., Held B., Lapidus A., Nolan M., Spring S., Yasawong M., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J.F., Goodwin L., Tapia R., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Brambilla E., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Sikorski J.,
RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Ignisphaera aggregans type strain (AQ1.S1).";
RL Stand. Genomic Sci. 3:66-75(2010).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CP002098; ADM28206.1; -; Genomic_DNA.
DR AlphaFoldDB; E0SQF0; -.
DR STRING; 583356.Igag_1403; -.
DR KEGG; iag:Igag_1403; -.
DR HOGENOM; CLU_015572_1_1_2; -.
DR BioCyc; IAGG583356:GHAH-1391-MONOMER; -.
DR Proteomes; UP000001304; 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 Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR00857; pyrC_multi; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000001304}.
FT DOMAIN 37..386
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 409 AA; 45960 MW; A5E9420C29217244 CRC64;
MDVAVVVRDG IVIESRGFVN KDICNNNMCI DLRSHGIALP GFIDIHTHLR GLHLSYKEDE
ETGTMAAARG GFTAVIDMPN TIPRIDNIDA LESKLRSLRE KAYVDYGIYI SPSNSIPRVN
SMLNVDGVIG VKIFPEDLKY VDIVLEILRR RNFDRLLIVH AEHPDYISEC EAGLRWRCRS
IDSELVALKI LGELSRRGDR IHVTHVTNTT TLRYARNMGF SVDTCPHYLY LSSEDERTLG
CIAKVNPPLR EPSVRDELLR SIKMFDAIST DHAPHSIEEK SKPFDECPAG IPSLDIAGSL
ILNLIHMDFL SIDDVIRLTS LGPAKIIGID RWGCIHEGCI ASYTIVDLDS EIIVDPSKFY
SKAKFSPYRG RRLKGVVKAT VIRGYVVFNG DNLDEKPVPE PLTKFMVRK
//
