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RIB7_KLULA
ID   RIB7_KLULA              Reviewed;         252 AA.
AC   Q6CJ61;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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   Name=RIB7; OrderedLocusNames=KLLA0F21120g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382126; CAG98736.1; -; Genomic_DNA.
DR   RefSeq; XP_456028.1; XM_456028.1.
DR   AlphaFoldDB; Q6CJ61; -.
DR   SMR; Q6CJ61; -.
DR   STRING; 28985.XP_456028.1; -.
DR   EnsemblFungi; CAG98736; CAG98736; KLLA0_F21120g.
DR   GeneID; 2895434; -.
DR   KEGG; kla:KLLA0_F21120g; -.
DR   eggNOG; ENOG502RZWZ; Eukaryota.
DR   HOGENOM; CLU_036590_5_0_1; -.
DR   InParanoid; Q6CJ61; -.
DR   OMA; ERWNCIE; -.
DR   UniPathway; UPA00275; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:EnsemblFungi.
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; IPR011549; RibD_C.
DR   InterPro; IPR002734; RibDG_C.
DR   Pfam; PF01872; RibD_C; 1.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   TIGRFAMs; TIGR00227; ribD_Cterm; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis.
FT   CHAIN           1..252
FT                   /note="2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-
FT                   phosphate reductase"
FT                   /id="PRO_0000135939"
FT   BINDING         80
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         189..193
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   252 AA;  28316 MW;  C8AD328CCE82349A CRC64;
     MPIQPLKKEL VSFLEPYMPE NAGVLGEQEK PYVILTYAQS LDARIAKIKG TRTIISHQET
     NTMTHYLRYK FDGIMLGCGT VLVDDPGLNC KWWPDDEPKP EHFAEHSPRP IILDPNGKWK
     FEGSKMKTLF DSGDGKAPIV VVKKLPEVVE ENVDYLVMQT NFTGKVDWHD LFIQLKSQFG
     LKSIMVEGGG IVINDLLQRP HLIDALVITV GATFLGSEGV EVSPLIEINL KDISWWKGTR
     DSVLCSRLVS HS
 
 
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