Reviewed, UniProtKB/Swiss-Prot Q8K9A4 (RIBD1_BUCAP)

Names and origin

Protein names

Recommended name:
    Diaminohydroxyphosphoribosylamino-pyrimidine deaminase
      Short name=DRAP deaminase
    EC=3.5.4.26
Alternative name(s):
    Riboflavin-specific deaminase

Gene names

Name:	ribD1
Ordered Locus Names:	BUsg_445

Organism

Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP]

Taxonomic identifier

98794 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H2O = 5-amino-6-(5-phosphoribosylamino)uracil + NH3.
Cofactor	Binds 1 zinc ion By similarity.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 6,7-dimethyl-8-(1-D-ribityl)lumazine from GTP: step 2/4.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity Inferred from electronic annotation. Source: InterPro diaminohydroxyphosphoribosylaminopyrimidine deaminase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 147	147	Diaminohydroxyphosphoribosylamino-pyrimidine deaminase		PRO_0000171726
Sites
	Active site	52	1	Proton donor By similarity
	Metal binding	50	1	Zinc; catalytic By similarity
	Metal binding	75	1	Zinc; catalytic By similarity
	Metal binding	84	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8K9A4-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: EBCCF068610EECF0	FASTA	147	16,233
	10 20 30 40 50 60 MKDRFYMTRA IKLSKLGEFT TSPNPNVGCV IVQNKKIVGE GWHKKYGENH AEINALNMAG 70 80 90 100 110 120 EKAKGSTAYI TLEPCNHFGK TPPCCDAIIQ SGIKNVIISS LDPNPKVSGK GVLYLRKKGI 130 140 SVKIGLMSKE SQKYNKGFFK RMRTGLP

References

[1]

"50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013218 Genomic DNA. Translation: AAM67988.1.
RefSeq	NP_660777.1.
3D structure databases
HSSP	HSSP built from PDB template 1UAQ based on UniProtKB Q12178.
ModBase	Search...
Genome annotation databases
GeneID	1005719.
GenomeReviews	Gene locus BUsg_445 in contig AE013218_GR.
KEGG	bas:BUsg445.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8K9A4.
OMA	Q8K9A4. PPVGCVL.
Enzyme and pathway databases
BioCyc	BAPH198804:BUSG445-MON.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR002125. CMP_dCMP_Zn_bd. IPR004794. Eubact_ribD. [Graphical view]
PANTHER	PTHR11079:SF10. Eubact_ribD. 1 hit.
Pfam	PF00383. dCMP_cyt_deam_1. 1 hit. [Graphical view]
TIGRFAMs	TIGR00326. eubact_ribD. 1 hit.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIBD1_BUCAP

Accession

Primary (citable) accession number: Q8K9A4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)