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
//