ID   E5WKX2_9BACI            Unreviewed;       279 AA.
AC   E5WKX2;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Dihydrouridine synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=HMPREF1013_03105 {ECO:0000313|EMBL:EFV76560.1};
OS   Bacillus sp. 2_A_57_CT2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=665959 {ECO:0000313|EMBL:EFV76560.1, ECO:0000313|Proteomes:UP000003283};
RN   [1] {ECO:0000313|EMBL:EFV76560.1, ECO:0000313|Proteomes:UP000003283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_A_57_CT2 {ECO:0000313|EMBL:EFV76560.1,
RC   ECO:0000313|Proteomes:UP000003283};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Larson L., Lui A., MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus sp. strain 2_A_57_CT2.";
RL   Submitted (DEC-2010) 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:EFV76560.1}.
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DR   EMBL; ACWD01000044; EFV76560.1; -; Genomic_DNA.
DR   RefSeq; WP_009333858.1; NZ_GL635753.1.
DR   AlphaFoldDB; E5WKX2; -.
DR   eggNOG; COG2513; Bacteria.
DR   HOGENOM; CLU_027389_2_3_9; -.
DR   Proteomes; UP000003283; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR42905:SF16; CARBOXYPHOSPHONOENOLPYRUVATE PHOSPHONOMUTASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_5G07230); 1.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE   4: Predicted;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003283}.
SQ   SEQUENCE   279 AA;  30768 MW;  21D054567258D18A CRC64;
     MSSKEQSLKA KTFHRLHQQS STFVLPNAWD VISAKMFEEC GFKAIGTTSA GIAASLGYLD
     GQSIPLNKMV ETIENIAKSV NVPVSADIEA GYGQTVEEVL ETVKAVAAAG AIGINLEDGT
     GDPNRPIFDI SSQEEKIAAI KELSESRNMP LFINARTDLY WLNIGDSSTR LQEAVSRAKA
     YQDAGADCIF IPGLTDRKII KKMREEVSCP INLLVDPEMP SLTELSEIRI ERLSCGSVPF
     RATLTYLRTI SEEIVNRQTF HQMTNGDVLS YKRLTEFIQ
//