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Database: UniProt
Entry: A0A1Q4EZK6_9SPHI
LinkDB: A0A1Q4EZK6_9SPHI
Original site: A0A1Q4EZK6_9SPHI 
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
//
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