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Q9PLJ6 (RIBD_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
Ordered Locus Names:TC_0103
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia/Chlamydophila group › Chlamydia

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Protein existenceInferred 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 deaminases family.

In the C-terminal section; belongs to the HTP reductase family.

Sequence caution

The sequence AAF38983.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 371371Riboflavin biosynthesis protein RibD
PRO_0000171717

Regions

Nucleotide binding301 – 3077NADP By similarity
Region1 – 150150Deaminase
Region151 – 371221Reductase

Sites

Active site571Proton donor By similarity
Metal binding551Zinc; catalytic By similarity
Metal binding801Zinc; catalytic By similarity
Metal binding891Zinc; catalytic By similarity
Binding site1591NADP; via amide nitrogen and carbonyl oxygen By similarity
Binding site1731Substrate By similarity
Binding site1751NADP By similarity
Binding site1891Substrate By similarity
Binding site2011NADP By similarity
Binding site2051NADP By similarity
Binding site2091Substrate; via amide nitrogen By similarity
Binding site2121Substrate By similarity
Binding site2301NADP By similarity
Binding site2991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PLJ6 [UniParc].

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

FASTA37140,912
        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

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002160 Genomic DNA. Translation: AAF38983.1. Different initiation.
PIRD81742.
RefSeqNP_296487.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PLJ6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1245633.
GenomeReviewsGene locus TC_0103 in contig AE002160_GR.
KEGGcmu:TC0103.
PATRIC20371560. VBIChlMur19118_0116.
TIGRTC_0103.

Phylogenomic databases

HOGENOMHBG668075.
PhylomeDBQ9PLJ6.
ProtClustDBCLSK871565.

Enzyme and pathway databases

BioCycCMUR243161:TC_0103-MONOMER.

Family and domain databases

InterProIPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR024072. DHFR-like_dom.
IPR004794. Eubact_RibD.
IPR011549. RibD_C.
IPR002734. RibDG_C.
[Graphical view]
Gene3DG3DSA:3.40.430.10. G3DSA:3.40.430.10. 1 hit.
KOK11752.
PANTHERPTHR11079:SF10. Eubact_ribD. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
PF01872. RibD_C. 1 hit.
[Graphical view]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
SSF53597. SSF53597. 1 hit.
TIGRFAMsTIGR00326. Eubact_ribD. 1 hit.
TIGR00227. RibD_Cterm. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRIBD_CHLMU
AccessionPrimary (citable) accession number: Q9PLJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: January 25, 2012
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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