RIB7_METTH
ID RIB7_METTH Reviewed; 216 AA.
AC O26337;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase;
DE Short=DAROPP reductase;
DE Short=DARP reductase;
DE EC=1.1.1.302;
DE AltName: Full=2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase;
DE AltName: Full=2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase;
DE Short=DARIPP synthase;
GN OrderedLocusNames=MTH_235;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Catalyzes an early step in riboflavin biosynthesis, the
CC NADPH-dependent reduction of the ribose side chain of 2,5-diamino-6-
CC ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding 2,5-diamino-6-
CC ribitylamino-4(3H)-pyrimidinone 5'-phosphate. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-
CC phosphate + NADP(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-
CC 4(3H)-one 5'-phosphate + H(+) + NADPH; Xref=Rhea:RHEA:27278,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58890, ChEBI:CHEBI:59545; EC=1.1.1.302;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-diamino-6-(1-D-ribitylamino)pyrimidin-4(3H)-one 5'-
CC phosphate + NAD(+) = 2,5-diamino-6-(1-D-ribosylamino)pyrimidin-4(3H)-
CC one 5'-phosphate + H(+) + NADH; Xref=Rhea:RHEA:27274,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58890, ChEBI:CHEBI:59545; EC=1.1.1.302;
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}.
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DR EMBL; AE000666; AAB84741.1; -; Genomic_DNA.
DR PIR; C69129; C69129.
DR RefSeq; WP_010875874.1; NC_000916.1.
DR PDB; 6P8C; X-ray; 2.07 A; A/B=1-216.
DR PDBsum; 6P8C; -.
DR AlphaFoldDB; O26337; -.
DR SMR; O26337; -.
DR STRING; 187420.MTH_235; -.
DR EnsemblBacteria; AAB84741; AAB84741; MTH_235.
DR GeneID; 1470196; -.
DR KEGG; mth:MTH_235; -.
DR PATRIC; fig|187420.15.peg.204; -.
DR HOGENOM; CLU_036590_4_1_2; -.
DR OMA; CECGQEV; -.
DR UniPathway; UPA00275; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase 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; IPR006401; Rib_reduct_arc.
DR InterPro; IPR011549; RibD_C.
DR InterPro; IPR002734; RibDG_C.
DR Pfam; PF01872; RibD_C; 1.
DR SUPFAM; SSF53597; SSF53597; 1.
DR TIGRFAMs; TIGR01508; rib_reduct_arch; 1.
DR TIGRFAMs; TIGR00227; ribD_Cterm; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome;
KW Riboflavin biosynthesis.
FT CHAIN 1..216
FT /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT phosphate reductase"
FT /id="PRO_0000135945"
FT BINDING 51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 79..82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 148..151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 29..40
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:6P8C"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:6P8C"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 162..172
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6P8C"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:6P8C"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:6P8C"
SQ SEQUENCE 216 AA; 23576 MW; 436561C089DF41A6 CRC64;
MRPYVILNAA MTLDGKIATA TGSSEISGEE DLRRVHELRR ECDAIMVGIN TVLADDPRLT
VHRVDAAPGD NPVRVVVDSM ARTPPHFRVL NDEAPTVIGV SESAPPERVA ELRKRAEVVV
AGTRRVDLHL LLERLHGMGI ERLMLEGGST LNYSMLTGGL VDEVRVCIAP MIVGGRDART
LVDGEGIDEM ADAIRLELKR SYTLGEDLIV EYTVKG
