RIBD2_BUCAP
ID RIBD2_BUCAP Reviewed; 217 AA.
AC Q8K9A3;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase;
DE EC=1.1.1.193;
DE AltName: Full=HTP reductase;
GN Name=ribD2; OrderedLocusNames=BUsg_446;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-
CC amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH;
CC Xref=Rhea:RHEA:17845, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58421, ChEBI:CHEBI:58453;
CC EC=1.1.1.193;
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 3/4.
CC -!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}.
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DR EMBL; AE013218; AAM67989.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8K9A3; -.
DR SMR; Q8K9A3; -.
DR STRING; 198804.BUsg_446; -.
DR EnsemblBacteria; AAM67989; AAM67989; BUsg_446.
DR KEGG; bas:BUsg_446; -.
DR eggNOG; COG1985; Bacteria.
DR HOGENOM; CLU_036590_1_2_6; -.
DR OMA; WFRAPIL; -.
DR UniPathway; UPA00275; UER00402.
DR Proteomes; UP000000416; Chromosome.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.430.10; -; 1.
DR InterPro; IPR024072; DHFR-like_dom_sf.
DR InterPro; IPR004794; Eubact_RibD.
DR InterPro; IPR011549; RibD_C.
DR InterPro; IPR002734; RibDG_C.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
DR TIGRFAMs; TIGR00326; eubact_ribD; 1.
DR TIGRFAMs; TIGR00227; ribD_Cterm; 1.
PE 3: Inferred from homology;
KW NADP; Oxidoreductase; Riboflavin biosynthesis.
FT CHAIN 1..217
FT /note="5-amino-6-(5-phosphoribosylamino)uracil reductase"
FT /id="PRO_0000171728"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 25345 MW; 65388CAAD7F6078F CRC64;
MSIDGRIAMK NGESRWITSK ESREDVQKFR AKSSAILTSS ATILNDDPLL NVRYKKFDKN
TLSTFPKKIF QQPIRIIIDS KNRVKKSHKI IQTKEKILLM RLKLDKEIWP ENTKQIIIKP
YKENIDLLCV LKFLGNLEIN NLWIEAGSTL SGCFLKLELI DEIIIYIAPK ILGHEAKPLF
IFNNQLKLFD CLKFDFKDIR QIGPDIRIKL EPKNKKF
