Riboflavin biosynthesis protein ribD

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Reviewed, UniProtKB/Swiss-Prot Q9PLJ6 (RIBD_CHLMU)

Last modified June 16, 2009. Version 54. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Riboflavin biosynthesis protein ribD
Including the following 2 domains:
    1- Recommended name:
            Diaminohydroxyphosphoribosylaminopyrimidine deaminase
                Short name=DRAP deaminase
              EC=3.5.4.26
        Alternative name(s):
            Riboflavin-specific deaminase
    2- Recommended name:
            5-amino-6-(5-phosphoribosylamino)uracil reductase
              EC=1.1.1.193
        Alternative name(s):
            HTP reductase

Gene names

Name:	ribD
Ordered Locus Names:	TC_0103

Organism

Chlamydia muridarum [Complete proteome] [HAMAP]

Taxonomic identifier

83560 [NCBI]

Taxonomic lineage

Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia

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Protein attributes

Sequence length	371 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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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-phosphoribitylamino)uracil + NADP⁺ = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH.
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. Cofactor biosynthesis; riboflavin biosynthesis; 6,7-dimethyl-8-(1-D-ribityl)lumazine from GTP: step 3/4.
Sequence similarities	In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminases family. In the C-terminal section; belongs to the HTP reductase family.

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Ontologies

Keywords
Biological process	Riboflavin biosynthesis
Ligand	Metal-binding NADP Zinc
Molecular function	Hydrolase Oxidoreductase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW 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 or NADPH binding 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 371

371

Riboflavin biosynthesis protein ribD

PRO_0000171717

Regions

Nucleotide binding

301 – 307

NADP By similarity

Region

1 – 150

150

Deaminase

Region

151 – 371

221

Reductase

Sites

Active site

Proton donor By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

Zinc; catalytic By similarity

Metal binding

Zinc; catalytic By similarity

Binding site

159

NADP; via amide nitrogen and carbonyl oxygen By similarity

Binding site

173

Substrate By similarity

Binding site

175

NADP By similarity

Binding site

189

Substrate By similarity

Binding site

201

NADP By similarity

Binding site

205

NADP By similarity

Binding site

209

Substrate; via amide nitrogen By similarity

Binding site

212

Substrate By similarity

Binding site

230

NADP By similarity

Binding site

299

Substrate By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9PLJ6-1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 2A37C047D233A1CA
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FASTA

371

40,912

        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

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References

[1]

"Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae AR39."
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.

Fraser C.M.
Nucleic Acids Res. 28:1397-1406(2000) [PubMed: 10684935] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MoPn / Nigg.

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Cross-references

Sequence databases
	AE002160 Genomic DNA. Translation: AAF38983.1. Different initiation.
PIR	D81742.
RefSeq	NP_296487.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1245633.
GenomeReviews	Gene locus TC_0103 in contig AE002160_GR.
KEGG	cmu:TC0103.
TIGR	TC_0103.
Phylogenomic databases
HOGENOM	Q9PLJ6.
Enzyme and pathway databases
BioCyc	CMUR243161:TC_0103-MON.
BRENDA	1.1.1.193. 256349. 3.5.4.26. 256349.
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]
PANTHER	PTHR11079:SF10. Eubact_ribD. 1 hit.
Pfam	PF00383. dCMP_cyt_deam_1. 1 hit. PF01872. RibD_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR00326. eubact_ribD. 1 hit. TIGR00227. ribD_Cterm. 1 hit.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. False negative. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

RIBD_CHLMU

Accession

Primary (citable) accession number: Q9PLJ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	April 27, 2001
Last modified:	June 16, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents