Diaminohydroxyphosphoribosylaminopyrimidine deaminase
     (DRAP deaminase)
     (EC 3.5.4.26)
     (Riboflavin-specific deaminase)
5-amino-6-(5-phosphoribosylamino)uracil reductase
     (EC 1.1.1.193)
     (HTP reductase)

Gene name

	Name:	ribD
	Synonyms:	ribG, ybaE
	OrderedLocusNames:	b0414, JW0404

From

Escherichia coli (strain K12)

[TaxID: 83333]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=K12; DOI=10.1007/BF00538702; PubMed=1406588 [NCBI, ExPASy, EBI, Israel, Japan] Taura T., Ueguchi C., Shiba K., Ito K.; "Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive growth of Escherichia coli and suppression of the secY24 mutation."; Mol. Gen. Genet. 234:429-432(1992).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; "Sequence of minutes 4-25 of Escherichia coli."; Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[5]	CHARACTERIZATION. PubMed=9068650 [NCBI, ExPASy, EBI, Israel, Japan] Richter G., Fischer M., Krieger C., Eberhardt S., Luttgen H., Gerstenschlager I., Bacher A.; "Biosynthesis of riboflavin: characterization of the bifunctional deaminase-reductase of Escherichia coli and Bacillus subtilis."; J. Bacteriol. 179:2022-2028(1997).

Comments

FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
CATALYTIC ACTIVITY: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H₂O = 5-amino-6-(5-phosphoribosylamino)uracil + NH₃.
CATALYTIC ACTIVITY: 5-amino-6-(5-phosphoribitylamino)uracil + NADP⁺ = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH.
COFACTOR: Zinc (By similarity).
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 6,7-dimethyl-8-(1-D-ribityl)lumazine from GTP: step 2/4 .
PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 6,7-dimethyl-8-(1-D-ribityl)lumazine from GTP: step 3/4 .
SIMILARITY: In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family.
SIMILARITY: In the C-terminal section; belongs to the HTP reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X64395; CAA45735.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U82664; AAB40170.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73517.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76194.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S26201; S26201.

RefSeq

AP_001064.1; -.
NP_414948.1; -.

3D structure databases

PDB

2G6V; X-ray; 2.60 A; A/B=2-367.	[ExPASy / RCSB / EBI]
2O7P; X-ray; 3.00 A; A/B=2-367.	[ExPASy / RCSB / EBI]
2OBC; X-ray; 3.00 A; A/B=2-367.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2G6V; -.
2O7P; -.
2OBC; -.

ModBase

P25539.

Protein-protein interaction databases

DIP

DIP:10708N; -.

Enzyme and pathway databases

BioCyc

EcoCyc:RIBOFLAVINSYNDEAM-MON; -.
MetaCyc:RIBOFLAVINSYNDEAM-MON; -.

Organism-specific databases

EchoBASE

EB1297; -.

EcoGene

EG11321; ribD.

Ontologies

GO:0008703;	Molecular function: 5-amino-6-(5-phosphoribosylamino)uracil reductase activity (inferred from electronic annotation from InterPro).
GO:0008835;	Molecular function: diaminohydroxyphosphoribosylaminopyrimidine deaminase activity (inferred from electronic annotation from InterPro).
GO:0050661;	Molecular function: NADP binding (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0009231;	Biological process: riboflavin biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016192; APOBEC/CMP_deaminase_Zn-bd.
IPR002125; CMP_dCMP_Zn_bd.
IPR004794; Eubact_ribD.
IPR011549; RibD_C.
IPR002734; RibDG_C.
Graphical view of domain structure.

PANTHER

PTHR11079:SF10; Eubact_ribD; 1.

Pfam

PF00383; dCMP_cyt_deam_1; 1.
PF01872; RibD_C; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00326; eubact_ribD; 1.
TIGR00227; ribD_Cterm; 1.

PROSITE

PS00903; CYT_DCMP_DEAMINASES; 1.

ProtoNet

P25539.

Genome annotation databases

GeneID

945620; -.

GenomeReviews

U00096_GR; b0414.
AP009048_GR; JW0404.

KEGG

ecj:JW0404; -.
eco:b0414; -.

Phylogenomic databases

HOGENOM

P25539; -.

Genome annotation databases

CMR

P25539; b0414.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Complete proteome; Hydrolase; Metal-binding; Multifunctional enzyme; NADP; Oxidoreductase; Riboflavin biosynthesis; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 367`	`367`	`Riboflavin biosynthesis protein ribD.`	`PRO_0000171721`
`REGION`	`1 145`	`145`	`Deaminase.`
`REGION`	`146 367`	`222`	`Reductase.`
`ACT_SITE`	`52 52`		`Proton donor (By similarity).`
`METAL`	`50 50`		`Zinc; catalytic (By similarity).`
`METAL`	`75 75`		`Zinc; catalytic (By similarity).`
`METAL`	`84 84`		`Zinc; catalytic (By similarity).`
`HELIX`	`1 14`	`14`
`HELIX`	`15 17`	`3`
`TURN`	`18 20`	`3`
`STRAND`	`28 33`	`6`
`STRAND`	`36 42`	`7`
`STRAND`	`46 48`	`3`
`HELIX`	`51 59`	`9`
`HELIX`	`60 63`	`4`
`STRAND`	`64 66`	`3`
`STRAND`	`68 72`	`5`
`HELIX`	`85 91`	`7`
`STRAND`	`96 100`	`5`
`HELIX`	`111 117`	`7`
`STRAND`	`122 124`	`3`
`HELIX`	`128 134`	`7`
`HELIX`	`136 143`	`8`
`STRAND`	`144 146`	`3`
`STRAND`	`148 156`	`9`
`HELIX`	`174 185`	`12`
`STRAND`	`187 193`	`7`
`HELIX`	`194 200`	`7`
`HELIX`	`208 210`	`3`
`HELIX`	`214 217`	`4`
`HELIX`	`221 223`	`3`
`STRAND`	`228 232`	`5`
`HELIX`	`243 245`	`3`
`STRAND`	`247 249`	`3`
`STRAND`	`251 257`	`7`
`STRAND`	`267 271`	`5`
`HELIX`	`281 290`	`10`
`STRAND`	`295 298`	`4`
`HELIX`	`302 311`	`10`
`STRAND`	`315 323`	`9`
`STRAND`	`349 356`	`8`
`STRAND`	`359 365`	`7`

Sequence information

Length: 367 AA [This is the length of the unprocessed precursor]

Molecular weight: 40338 Da [This is the MW of the unprocessed precursor]

CRC64: B19CEF474D48D14D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQDEYYMARA LKLAQRGRFT THPNPNVGCV IVKDGEIVGE GYHQRAGEPH AEVHALRMAG 

        70         80         90        100        110        120 
EKAKGATAYV TLEPCSHHGR TPPCCDALIA AGVARVVASM QDPNPQVAGR GLYRLQQAGI 

       130        140        150        160        170        180 
DVSHGLMMSE AEQLNKGFLK RMRTGFPYIQ LKLGASLDGR TAMASGESQW ITSPQARRDV 

       190        200        210        220        230        240 
QLLRAQSHAI LTSSATVLAD DPALTVRWSE LDEQTQALYP QQNLRQPIRI VIDSQNRVTP 

       250        260        270        280        290        300 
VHRIVQQPGE TWFARTQEDS REWPETVRTL LIPEHKGHLD LVVLMMQLGK QQINSIWVEA 

       310        320        330        340        350        360 
GPTLAGALLQ AGLVDELIVY IAPKLLGSDA RGLCTLPGLE KLADAPQFKF KEIRHVGPDV 


CLHLVGA

P25539 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools