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MAIZE:RIBRX

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Species (Taxon ID) Zea mays (Maize). (4577)
Gene Name(s) PYRR
Protein Name(s) Riboflavin biosynthesis protein PYRR, chloroplastic

Inactive diaminohydroxyphosphoribosylaminopyrimidine deaminase DRAP deaminase Riboflavin-specific deaminase 5-amino-6-(5-phosphoribosylamino)uracil reductase HTP reductase Riboflavin biosynthesis intermediates N-glycosidase (ECO:0000305 with PMID:25431972[1])

External Links
UniProt K7WIZ6
EMBL JX838796
RefSeq NP_001266474.1
UniGene Zm.126241
ProteinModelPortal K7WIZ6
STRING 4577.GRMZM2G090068_P01
PaxDb K7WIZ6
EnsemblPlants [example_ID GRMZM2G090068_T01]
GeneID 101202729
Gramene GRMZM2G090068_T01
KEGG zma:101202729
eggNOG ENOG410IU3U
ENOG410JSA8
COG0117
COG1985
COG3236
KO K11752
OMA DCYGDST
UniPathway UPA00275
Proteomes UP000007305
GO GO:0009507
GO:0008703
GO:0008835
GO:0004159
GO:0016799
GO:0050661
GO:0008270
GO:1901135
GO:0009658
GO:0046443
GO:0009644
GO:0009231
Gene3D 3.40.430.10
InterPro IPR012816
IPR002125
IPR016193
IPR024072
IPR004794
IPR011549
IPR002734
Pfam PF08719
PF01872
SUPFAM SSF53597
SSF53927
TIGRFAMs TIGR00326
TIGR00227
TIGR02464
PROSITE PS51747

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004159

dihydrouracil dehydrogenase (NAD+) activity

PMID:23150645[2]

ECO:0000314

F

Figure 3B shows that ZmPyrR complements reductase but not deaminase function of E. coli RibD.

Figure 4A shows the disappearance of 5-amino-6-ribosylamino-2,4(1H,3H)-pyrimidinedione 5’-P and Figure 4B shows the appearance of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5’-P in recombinant maize PyR. E. coli RibA, demonstrating pyrimidine reductase activity in vitro.

complete
CACAO 7870

GO:0009507

chloroplast

PMID:23150645[2]

ECO:0000314

C

Figure 6 shows radiolabeled Maize PyrR plastid localization.

complete
CACAO 7873

enables

GO:0016799

hydrolase activity, hydrolyzing N-glycosyl compounds

PMID:25431972[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:1901135

carbohydrate derivative metabolic process

PMID:25431972[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

PMID:23150645[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004159

dihydrouracil dehydrogenase (NAD+) activity

PMID:23150645[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:1901135

carbohydrate derivative metabolic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9STY4
araport11:AT3G47390.1

P

Seeded From UniProt

complete

involved_in

GO:0046443

FAD metabolic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9STY4
araport11:AT3G47390.1

P

Seeded From UniProt

complete

enables

GO:0016799

hydrolase activity, hydrolyzing N-glycosyl compounds

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9STY4
araport11:AT3G47390.1

F

Seeded From UniProt

complete

involved_in

GO:0009658

chloroplast organization

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9STY4
araport11:AT3G47390.1

P

Seeded From UniProt

complete

involved_in

GO:0009644

response to high light intensity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9STY4
araport11:AT3G47390.1

P

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9STY4
araport11:AT3G47390.1

C

Seeded From UniProt

complete

enables

GO:0008703

5-amino-6-(5-phosphoribosylamino)uracil reductase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:Q9STY4
araport11:AT3G47390.1

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016193

F

Seeded From UniProt

complete

enables

GO:0008703

5-amino-6-(5-phosphoribosylamino)uracil reductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002734
InterPro:IPR011549

F

Seeded From UniProt

complete

enables

GO:0008835

diaminohydroxyphosphoribosylaminopyrimidine deaminase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004794

F

Seeded From UniProt

complete

involved_in

GO:0009231

riboflavin biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002734
InterPro:IPR004794
InterPro:IPR011549

P

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011549

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR002734
InterPro:IPR004794
InterPro:IPR011549

P

Seeded From UniProt

complete

enables

GO:0008703

5-amino-6-(5-phosphoribosylamino)uracil reductase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.1.1.193

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326
UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0009507

chloroplast

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0150
UniProtKB-SubCell:SL-0049

C

Seeded From UniProt

complete

part_of

GO:0009536

plastid

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0934

C

Seeded From UniProt

complete

involved_in

GO:0009231

riboflavin biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00275

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Frelin, O et al. (2015) A directed-overflow and damage-control N-glycosidase in riboflavin biosynthesis. Biochem. J. 466 137-45 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Hasnain, G et al. (2013) Identification and characterization of the missing pyrimidine reductase in the plant riboflavin biosynthesis pathway. Plant Physiol. 161 48-56 PubMed GONUTS page