O66534 (RIBD_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Riboflavin biosynthesis protein RibD

Including the following 2 domains:

1. Diaminohydroxyphosphoribosylaminopyrimidine deaminase
   Short name=DRAP deaminase
   EC=3.5.4.26
   Alternative name(s):
   Riboflavin-specific deaminase
2. 5-amino-6-(5-phosphoribosylamino)uracil reductase
   EC=1.1.1.193
   Alternative name(s):
   HTP reductase

Gene names

Name:	ribD
Synonyms:	ribG
Ordered Locus Names:	aq_138

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (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. 5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP+ = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH.
Cofactor	Binds 1 zinc ion By similarity.
Pathway	Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4. Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4.
Sequence similarities	In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family. In the C-terminal section; belongs to the HTP reductase family.

Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	Metal-binding NADP Zinc
Molecular function	Hydrolase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme Reference 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: EC NADP binding Inferred from electronic annotation. Source: InterPro diaminohydroxyphosphoribosylaminopyrimidine deaminase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Riboflavin biosynthesis protein RibD		PRO_0000171713
Regions
	Nucleotide binding	292 – 298	7	NADP By similarity
	Region	1 – 148	148	Deaminase
	Region	149 – 356	208	Reductase
Sites
	Active site	55	1	Proton donor By similarity
	Metal binding	53	1	Zinc; catalytic By similarity
	Metal binding	78	1	Zinc; catalytic By similarity
	Metal binding	87	1	Zinc; catalytic By similarity
	Binding site	157	1	NADP; via amide nitrogen and carbonyl oxygen By similarity
	Binding site	171	1	Substrate By similarity
	Binding site	173	1	NADP By similarity
	Binding site	187	1	Substrate By similarity
	Binding site	199	1	NADP By similarity
	Binding site	203	1	NADP By similarity
	Binding site	207	1	Substrate; via amide nitrogen By similarity
	Binding site	210	1	Substrate By similarity
	Binding site	290	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O66534 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 7775515B1E4D02BD	FASTA	356	39,629
	10 20 30 40 50 60 MIREIDKNYM KLALSLAKKR KGYTHPNPTV GAVVVKEGKI VGLGYHEKAG KPHAEVMALG 70 80 90 100 110 120 QAGEKAKGAT LYVTLEPCTH FGRTPPCTDA IIRSGIKRVV VATLDPNPLM SGKGVEKLRN 130 140 150 160 170 180 AGIEVDVGVC EEEARELNED FFTYITQERP YITLKWAQTL DGKLATLTGS SKWITSKESR 190 200 210 220 230 240 KVAHILRREA TAVLVGVNTV IKDDPHLTVR FVPTEKQPVR IILDPELEVP LSAKVLNTEE 250 260 270 280 290 300 APTIVITKKE NEKAEKLKEK GVQVLILKGF NLKNILKKLK ELEIMHLMVE GGPRTLTSFL 310 320 330 340 350 KEGFFDRIVV FIAPKIMGEG LSIGDLGIRS IEESLKVRKK KVENLGEDLV IFFKRY

References

[1]

"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC06487.1.
PIR	C70313.
RefSeq	NP_213094.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O66534.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1192677.
GenomeReviews	Gene locus aq_138 in contig AE000657_GR.
KEGG	aae:aq_138.
NMPDR	fig|224324.1.peg.109.
PATRIC	20957954. VBIAquAeo85532_0117.
Phylogenomic databases
HOGENOM	HBG668075.
OMA	THILRAQ.
PhylomeDB	O66534.
ProtClustDB	CLSK2748247.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_138-MONOMER.
Family and domain databases
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR002125. CMP_dCMP_Zn-bd. IPR016193. Cytidine_deaminase-like. IPR024072. DHFR-like_dom. IPR004794. Eubact_RibD. IPR011549. RibD_C. IPR002734. RibDG_C. [Graphical view]
Gene3D	G3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit.
KO	K11752.
Pfam	PF00383. dCMP_cyt_deam_1. 1 hit. PF01872. RibD_C. 1 hit. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit. SSF53597. SSF53597. 1 hit.
TIGRFAMs	TIGR00326. Eubact_ribD. 1 hit. TIGR00227. RibD_Cterm. 1 hit.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RIBD_AQUAE

Accession

Primary (citable) accession number: O66534

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program