RIBD2_BUCAI
ID RIBD2_BUCAI Reviewed; 207 AA.
AC P57534;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=BU462;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB13159.1; -; Genomic_DNA.
DR RefSeq; NP_240273.1; NC_002528.1.
DR RefSeq; WP_009874414.1; NC_002528.1.
DR AlphaFoldDB; P57534; -.
DR SMR; P57534; -.
DR STRING; 107806.10039125; -.
DR EnsemblBacteria; BAB13159; BAB13159; BAB13159.
DR KEGG; buc:BU462; -.
DR PATRIC; fig|107806.10.peg.471; -.
DR eggNOG; COG1985; Bacteria.
DR HOGENOM; CLU_036590_1_2_6; -.
DR OMA; WFRAPIL; -.
DR UniPathway; UPA00275; UER00402.
DR Proteomes; UP000001806; 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; Reference proteome; Riboflavin biosynthesis.
FT CHAIN 1..207
FT /note="5-amino-6-(5-phosphoribosylamino)uracil reductase"
FT /id="PRO_0000171727"
FT BINDING 6
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 8
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 207 AA; 23942 MW; DAC973284089D76A CRC64;
MRNGDSKWIT SKQARQDVQK FRAKSSVILS SSSTILSDNP LLNVRYKELD KKTLSIFPNK
IFQHPIRVII DSKNRVQPSH NIIKTKGKIW LIRLKSDRKI WPKNTTQIIE KDHNKKINIF
SLLKFLGQSE INNVWIEAGS TLSGFLLNSY LIDELIIYMA PKILGHEAKP LCMIYEKLKI
SNSLQFKFKN ICQIGPDIRL ILSPKKI
