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Database: UniProt
Entry: K9E103_9BURK
LinkDB: K9E103_9BURK
Original site: K9E103_9BURK 
ID   K9E103_9BURK            Unreviewed;       427 AA.
AC   K9E103;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Dihydroorotase, multifunctional complex type {ECO:0000313|EMBL:EKU83105.1};
GN   ORFNames=HMPREF9710_01503 {ECO:0000313|EMBL:EKU83105.1};
OS   Massilia timonae CCUG 45783.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU83105.1, ECO:0000313|Proteomes:UP000009874};
RN   [1] {ECO:0000313|EMBL:EKU83105.1, ECO:0000313|Proteomes:UP000009874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU83105.1,
RC   ECO:0000313|Proteomes:UP000009874};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Massilia timonae CCUG 45783.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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:EKU83105.1}.
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DR   EMBL; AGZI01000017; EKU83105.1; -; Genomic_DNA.
DR   RefSeq; WP_005665327.1; NZ_JH992922.1.
DR   AlphaFoldDB; K9E103; -.
DR   STRING; 47229.LO55_2099; -.
DR   PATRIC; fig|883126.3.peg.1521; -.
DR   eggNOG; COG0044; Bacteria.
DR   HOGENOM; CLU_015572_1_0_4; -.
DR   OrthoDB; 9803027at2; -.
DR   Proteomes; UP000009874; Unassembled WGS sequence.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd01317; DHOase_IIa; 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; IPR013108; Amidohydro_3.
DR   InterPro; IPR004722; DHOase.
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; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009874}.
FT   DOMAIN          178..425
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   427 AA;  45191 MW;  1C54B7752C924B34 CRC64;
     MKLHIKNGRV IDPANGIDAA QDLFIADGRI AALGAAPQGF SADQTIDASG LVVAPGLIDL
     SARLREPGYE YKATLESELQ AAMQGGVTTL VCPPDTDPVL DEPGLVEMLK HRARMLDQAN
     VHPLGALTVG LKGQALTEMA ELTEAGCIGF AQAEEPILDT TVLLRAMQYA KTFGYTVWLR
     PQDAHIGRGG VAHSGPLASR LGLSGVPVMS ETIALHTIFE LMRATGARVH LCRISSAAGL
     ELIRAAKKEG LDLSVDVGVH HLHMTDADIG FFDSNARLTP PLRSQRDRDA IRAAVLDGTV
     DAVCSDHTPV DDDEKLLPFG EASPGATGLE LLLSLTLKWA QDQQDADKAL ALALGRITHD
     AARIAGLPAG TLGVGAAADV VLFDPDARWK VEGKTLASQG KHTPFLGYEL AGQVKATIVR
     GRVAYQR
//
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