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UniProtKB/Swiss-Prot entry Q9Z735


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RIBD_CHLPN
Primary accession number Q9Z735
Secondary accession number Q9JQ54
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 62)
Name and origin of the protein
Protein name Riboflavin biosynthesis protein ribD
Synonyms None
Includes 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
Synonyms: ribG
OrderedLocusNames: CPn_0871, CP_0998, CpB0900
From
Chlamydia pneumoniae (Chlamydophila pneumoniae) [TaxID: 83558] [HAMAP proteome]
Taxonomy Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CWL029;
DOI=10.1038/7716; PubMed=10192388 [NCBI, ExPASy, EBI, Israel, Japan]
Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W., Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
"Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
Nat. Genet. 21:385-389(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AR39;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=J138;
DOI=10.1093/nar/28.12.2311; PubMed=10871362 [NCBI, ExPASy, EBI, Israel, Japan]
Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
"Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA.";
Nucleic Acids Res. 28:2311-2314(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=TW-183;
Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
"The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
Comments
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
AE001363; AAD19009.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE002161; AAF38776.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000008; BAA99079.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017160; AAP98829.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR E86599; E86599.
G72026; G72026.
RefSeq NP_225066.1; -.
NP_300928.1; -.
NP_445535.1; -.
NP_877172.1; -.
3D structure databases
ModBase Q9Z735.
Enzyme and pathway databases
BioCyc CPNE115711:CP_0998-MON; -.
CPNE115713:CPN0871-MON; -.
CPNE138677:CPJ0871-MON; -.
CPNE182082:CPB0900-MON; -.
Ontologies
GO
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; 1.
ProtoNet Q9Z735.
Genome annotation databases
GeneID 1467579; -.
895231; -.
919634; -.
963471; -.
GenomeReviews AE002161_GR; CP_0998.
AE009440_GR; CpB0900.
AE001363_GR; CPn_0871.
BA000008_GR; ribD.
KEGG cpa:CP0998; -.
cpn:CPn0871; -.
cpt:CpB0900; -.
TIGR CP_0998; -.
Phylogenomic databases
HOGENOM Q9Z735; -.
Other
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
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   376  376     Riboflavin biosynthesis protein ribD. PRO_0000171718
REGION   1   150  150     Deaminase. 
REGION   151   376  226     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: 376 AA [This is the length of the unprocessed precursor] Molecular weight: 41209 Da [This is the MW of the unprocessed precursor] CRC64: A05F069E0F127B07 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEDFSEQQLF FMRRAIEIGE KGRITAPPNP WVGCVVVQEN RIIGEGFHAY AGGPHAEELA 

        70         80         90        100        110        120 
IQNASMPISG SDVYVSLEPC SHFGSCPPCA NLLIKHKVSR VFVALVDPDP KVAGQGIAML 

       130        140        150        160        170        180 
RQAGIQVYVG IGESEAQASL QPYLYQRTHN FPWTILKSAA SVDGQVADSQ GKSQWITCPE 

       190        200        210        220        230        240 
ARHDVGKLRA ESQAILVGSR TVLSDDPWLT ARQPQGMLYP KQPLRVVLDS RGSVPPTSKV 

       250        260        270        280        290        300 
FDKTSPTLYV TTERCPENYI KVLDSLDVPV LLTESTPSGV DLHKVYEYLA QKKILQVLVE 

       310        320        330        340        350        360 
GGTTLHTSLL KERFVNSLVL YSGPMILGDQ KRPLVGVLGN LLESASPLTL KSSQILGNSL 

       370 
KVVWEISPQV FEPIRN 

Q9Z735 in FASTA format

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