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
	OrderedLocusNames:	bbp_408

From

Buchnera aphidicola subsp. Baizongia pistaciae

[TaxID: 135842]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0235981100; PubMed=12522265 [NCBI, ExPASy, EBI, Israel, Japan]
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
"Reductive genome evolution in Buchnera aphidicola.";
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).

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 (By similarity).
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

AE016826; AAO27119.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_778014.1; -.

3D structure databases

ModBase

Q89AB0.

Enzyme and pathway databases

BioCyc

BAPH224915:BBP_408-MON; -.

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.

Genome annotation databases

GeneID

1058488; -.

GenomeReviews

AE016826_GR; bbp_408.

KEGG

bab:bbp408; -.

Phylogenomic databases

HOGENOM

Q89AB0; -.

Genome annotation databases

CMR

Q89AB0; bbp_408.

Other

UniRef

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

Keywords

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`	`1 372`	`372`	`Riboflavin biosynthesis protein ribD.`	`PRO_0000171716`
`REGION`	`1 145`	`145`	`Deaminase.`
`REGION`	`146 372`	`227`	`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).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 41598 Da [This is the MW of the unprocessed precursor]

CRC64: 6BB07CE7E9016C7A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKDIFYMKKA IKLAKKGSLT TSPNPNVGCI IVNNNIIVGS GWHKKTGMKH AEIYALKTSG 

        70         80         90        100        110        120 
EKAKGATAYI TLEPCSHFGK TPPCCVALTK YGISRVVIAT LDPNPKVSGN GVKWLKKHGI 

       130        140        150        160        170        180 
LVTIGTLSKE SIKINKGFFQ RMTTGIPWIK LKLASSIDGR TALNNGKSKW ITSDKARHDV 

       190        200        210        220        230        240 
QHVREKSDAI ISSSETILFD NPLLTVRNTN NNDNNQKLLK HSKTFLKQPI RVIIDSKNRI 

       250        260        270        280        290        300 
TPSHKCIKQP GLLFLIRIHS DNNIWPSHIK QIILNNKSKK IDLIDLVKML AKYQINNILI 

       310        320        330        340        350        360 
EAGPSLSSSF LKLNIINELI IYIAPKILGN YAKPLFFLEN YSNLSDVPQF KFEKITQIGK 

       370 
DLKLILTKHN SS

Q89AB0 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