ID A0A0D6P4N2_9PROT Unreviewed; 443 AA.
AC A0A0D6P4N2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:GAN76715.1};
GN ORFNames=Asru_0150_02 {ECO:0000313|EMBL:GAN76715.1};
OS Acidisphaera rubrifaciens HS-AP3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidisphaera.
OX NCBI_TaxID=1231350 {ECO:0000313|EMBL:GAN76715.1, ECO:0000313|Proteomes:UP000032680};
RN [1] {ECO:0000313|EMBL:GAN76715.1, ECO:0000313|Proteomes:UP000032680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-AP3 {ECO:0000313|EMBL:GAN76715.1,
RC ECO:0000313|Proteomes:UP000032680};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidisphaera rubrifaciens HS-AP3.";
RL Submitted (NOV-2012) 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:GAN76715.1}.
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DR EMBL; BANB01000150; GAN76715.1; -; Genomic_DNA.
DR RefSeq; WP_048860588.1; NZ_BANB01000150.1.
DR AlphaFoldDB; A0A0D6P4N2; -.
DR OrthoDB; 9775759at2; -.
DR Proteomes; UP000032680; 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 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 NCBIfam; TIGR00857; pyrC_multi; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF4; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 2.
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:UP000032680}.
FT DOMAIN 54..127
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 284..419
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 443 AA; 48064 MW; AF6BF132FD5D9C02 CRC64;
MSDHYDLLIR NGVCILPWGE AATDIGVRDG RIATLSAPAG ASAEAVFDAR HLHVLPGLID
PHVHLRDPGD ATVESIATGT RAALLGGLTA VFDMPNTSPA ITDAERLAWK QDHAERVAWC
DIGLYVGATK ANAEALASLE TARGVCAVKV FAGSSTGDLL VEDDASIARV MRHGRRRIAF
HSEDEYRLRA RAPLFNRGDP YRCHMEWRDE ECAALGTRRI IALARETRRP AHILHVSTAA
EYAYLRDCRD IATSEVLVNH LTQIAPEAYD TLGGYAVMNP PIRDRRHYDA AWAAVADGTI
DTIGSDHAPH PRAKKELPWP DCAAGLTGVQ TLVPVMLDHV NAGRLTLGRM VDLMAAGPAR
VYGAIGKGRI AAGYDADFTI VDMRRQRTIE NDWIASPCGW TPFAGKRVTG WPVATVLRGG
IAMRDDAIIG APRGRLVRFL DTA
//
