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:	TC_0103

From

Chlamydia muridarum

[TaxID: 83560]

[HAMAP proteome]

Taxonomy

Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=MoPn / Nigg;
DOI=10.1093/nar/28.6.1397; PubMed=10684935 [NCBI, ExPASy, EBI, Israel, Japan]
Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39.";
Nucleic Acids Res. 28:1397-1406(2000).

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 deaminases 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

AE002160; AAF38983.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D81742; D81742.

RefSeq

NP_296487.1; -.

3D structure databases

ModBase

Q9PLJ6.

Enzyme and pathway databases

BioCyc

CMUR243161:TC_0103-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; FALSE_NEG.

Genome annotation databases

GeneID

1245633; -.

GenomeReviews

AE002160_GR; TC_0103.

KEGG

cmu:TC0103; -.

TIGR

TC_0103; -.

Phylogenomic databases

HOGENOM

Q9PLJ6; -.

Other

ProtoNet

Q9PLJ6.

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`	`1 371`	`371`	`Riboflavin biosynthesis protein ribD.`	`PRO_0000171717`
`REGION`	`1 150`	`150`	`Deaminase.`
`REGION`	`151 371`	`221`	`Reductase.`
`ACT_SITE`	`57 57`		`Proton donor (By similarity).`
`METAL`	`55 55`		`Zinc; catalytic (By similarity).`
`METAL`	`80 80`		`Zinc; catalytic (By similarity).`
`METAL`	`89 89`		`Zinc; catalytic (By similarity).`

Sequence information

Length: 371 AA [This is the length of the unprocessed precursor]

Molecular weight: 40912 Da [This is the MW of the unprocessed precursor]

CRC64: 2A37C047D233A1CA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEVSSEQQLF FMREAVALGE RGRIFAPPNP WVGCVIVKNG CIIGRGWHKG IGSPHAEVCA 

        70         80         90        100        110        120 
FQDQTSSLVG ADVYVTLEPC CHFGRTPPCV DLLIKSKVSS VYIALLDPDP RVCKRGVARL 

       130        140        150        160        170        180 
KEAGISVYVG IGHEEAKASL QPYLHQRETG LPWVVMKTAA SLDGQTSDRR GISQWISGEQ 

       190        200        210        220        230        240 
ARLDVGRLRA ESQAVIVGSR TVCLDNPRLS ARMPSGDLYE RQPLRVVVDS RGSVPLDARV 

       250        260        270        280        290        300 
WNPDSGNVLL ATTEQCSKEH IQKLEDRGVE VWKSSPQQVD LKRLLQYLAE KGCLQVLVEG 

       310        320        330        340        350        360 
GARLHSAFWR EHLVNAGVIY WGPKFLGDQG SPMLRDLQLC LDNAEHVKIT KTFLVGDSVK 

       370 
TCFECVGRED G

Q9PLJ6 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