ID A0A1Q4EZK6_9SPHI Unreviewed; 463 AA.
AC A0A1Q4EZK6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:OJY81240.1};
GN ORFNames=BGP14_07790 {ECO:0000313|EMBL:OJY81240.1};
OS Sphingobacteriales bacterium 44-15.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY81240.1, ECO:0000313|Proteomes:UP000186250};
RN [1] {ECO:0000313|EMBL:OJY81240.1, ECO:0000313|Proteomes:UP000186250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-15 {ECO:0000313|EMBL:OJY81240.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJY81240.1}.
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DR EMBL; MKWG01000045; OJY81240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4EZK6; -.
DR STRING; 1895837.BGP14_07790; -.
DR Proteomes; UP000186250; 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; IPR006680; Amidohydro-rel.
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 Pfam; PF01979; Amidohydro_1; 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}.
FT DOMAIN 52..441
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 463 AA; 52212 MW; 780BFB36F186F237 CRC64;
MQNYLLKNIT VVNEENISVK DVLLKNGRIE KIAGNIQPGS SVQEINGEGK HLLPGVIDDQ
VHFREPGLTH KATIYTESKA AVAGGVTSFM EMPNTIPNAL TIDLLEEKYA IASRSALANY
SFFMGTSNSN AEEVLKVNNY RDSICGVKIF MGSSTGNMLV DNYLTLDRLF RESEVLIATH
CEDEKIIKAN YEKIKKEKGA LSPADHPLIR NEDACFESSF TAIQFAKKYN SRLHILHIST
EKELQLFTNM MPLSDKRITC EVCVHHLHFS SEDYNRLGYL IKCNPAIKAP HNRAALWQAL
NDDRIDVIAT DHAPHTLEEK GYTRDADGSL IIKEGISYEQ AHAGLPLVQH PLLLLLHYYK
EGKIPLEKIV RKMSHSVADI YRIRDRGYIR EGYWADLVMA DLNKSTVVSA DNIAYKCGWS
PLEGFSFPAA ITHTFMNGTL VYENYGNGRW NESHRGMRLA FDR
//