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Riboflavin biosynthesis protein RibD [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)]

 RIBD_CHLPN              Reviewed;         376 AA.
Q9Z735; Q9JQ54;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
28-MAR-2018, entry version 127.
RecName: Full=Riboflavin biosynthesis protein RibD;
Includes:
RecName: Full=Diaminohydroxyphosphoribosylaminopyrimidine deaminase;
Short=DRAP deaminase;
EC=3.5.4.26;
AltName: Full=Riboflavin-specific deaminase;
Includes:
RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase;
EC=1.1.1.193;
AltName: Full=HTP reductase;
Name=ribD; Synonyms=ribG;
OrderedLocusNames=CPn_0871, CP_0998, CpB0900;
Chlamydia pneumoniae (Chlamydophila pneumoniae).
Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
Chlamydia/Chlamydophila group; Chlamydia.
NCBI_TaxID=83558;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CWL029;
PubMed=10192388; DOI=10.1038/7716;
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;
PubMed=10684935; DOI=10.1093/nar/28.6.1397;
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;
PubMed=10871362; DOI=10.1093/nar/28.12.2311;
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.
-!- 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 + H(2)O = 5-amino-6-(5-
phosphoribosylamino)uracil + NH(3).
-!- CATALYTIC ACTIVITY: 5-amino-6-(5-phospho-D-ribitylamino)uracil +
NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion. {ECO:0000250};
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
6-(D-ribitylamino)uracil from GTP: step 2/4.
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
6-(D-ribitylamino)uracil from GTP: step 3/4.
-!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
deoxycytidylate deaminase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the HTP
reductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE001363; AAD19009.1; -; Genomic_DNA.
EMBL; AE002161; AAF38776.1; -; Genomic_DNA.
EMBL; BA000008; BAA99079.1; -; Genomic_DNA.
EMBL; AE009440; AAP98829.1; -; Genomic_DNA.
PIR; E86599; E86599.
PIR; G72026; G72026.
RefSeq; NP_225066.1; NC_000922.1.
RefSeq; WP_010883506.1; NZ_LN847257.1.
ProteinModelPortal; Q9Z735; -.
SMR; Q9Z735; -.
STRING; 182082.CpB0900; -.
EnsemblBacteria; AAD19009; AAD19009; CPn_0871.
EnsemblBacteria; AAF38776; AAF38776; CP_0998.
EnsemblBacteria; AAP98829; AAP98829; CpB0900.
EnsemblBacteria; BAA99079; BAA99079; BAA99079.
GeneID; 895231; -.
KEGG; cpa:CP_0998; -.
KEGG; cpj:ribD; -.
KEGG; cpn:CPn0871; -.
KEGG; cpt:CpB0900; -.
PATRIC; fig|115713.3.peg.951; -.
eggNOG; ENOG4105D1W; Bacteria.
eggNOG; COG0117; LUCA.
eggNOG; COG1985; LUCA.
HOGENOM; HOG000257442; -.
KO; K11752; -.
OMA; YIILKWA; -.
OrthoDB; POG091H01D3; -.
UniPathway; UPA00275; UER00401.
UniPathway; UPA00275; UER00402.
Proteomes; UP000000583; Chromosome.
Proteomes; UP000000801; Chromosome.
GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:UniProtKB-EC.
GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.430.10; -; 1.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
InterPro; IPR024072; DHFR-like_dom_sf.
InterPro; IPR004794; Eubact_RibD.
InterPro; IPR011549; RibD_C.
InterPro; IPR002734; RibDG_C.
Pfam; PF00383; dCMP_cyt_deam_1; 1.
Pfam; PF01872; RibD_C; 1.
PIRSF; PIRSF006769; RibD; 1.
SUPFAM; SSF53597; SSF53597; 1.
SUPFAM; SSF53927; SSF53927; 1.
TIGRFAMs; TIGR00326; eubact_ribD; 1.
TIGRFAMs; TIGR00227; ribD_Cterm; 1.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
3: Inferred from homology;
Complete proteome; Hydrolase; Metal-binding; Multifunctional enzyme;
NADP; Oxidoreductase; Reference proteome; Riboflavin biosynthesis;
Zinc.
CHAIN 1 376 Riboflavin biosynthesis protein RibD.
/FTId=PRO_0000171718.
DOMAIN 6 128 CMP/dCMP-type deaminase.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
NP_BIND 302 308 NADP. {ECO:0000250}.
REGION 1 150 Deaminase.
REGION 151 376 Reductase.
ACT_SITE 57 57 Proton donor. {ECO:0000250}.
METAL 55 55 Zinc; catalytic. {ECO:0000250}.
METAL 80 80 Zinc; catalytic. {ECO:0000250}.
METAL 89 89 Zinc; catalytic. {ECO:0000250}.
BINDING 159 159 NADP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 173 173 Substrate. {ECO:0000250}.
BINDING 175 175 NADP. {ECO:0000250}.
BINDING 189 189 Substrate. {ECO:0000250}.
BINDING 201 201 NADP. {ECO:0000250}.
BINDING 205 205 NADP. {ECO:0000250}.
BINDING 209 209 Substrate; via amide nitrogen.
{ECO:0000250}.
BINDING 212 212 Substrate. {ECO:0000250}.
BINDING 230 230 NADP. {ECO:0000250}.
BINDING 300 300 Substrate. {ECO:0000250}.
SEQUENCE 376 AA; 41209 MW; A05F069E0F127B07 CRC64;
MEDFSEQQLF FMRRAIEIGE KGRITAPPNP WVGCVVVQEN RIIGEGFHAY AGGPHAEELA
IQNASMPISG SDVYVSLEPC SHFGSCPPCA NLLIKHKVSR VFVALVDPDP KVAGQGIAML
RQAGIQVYVG IGESEAQASL QPYLYQRTHN FPWTILKSAA SVDGQVADSQ GKSQWITCPE
ARHDVGKLRA ESQAILVGSR TVLSDDPWLT ARQPQGMLYP KQPLRVVLDS RGSVPPTSKV
FDKTSPTLYV TTERCPENYI KVLDSLDVPV LLTESTPSGV DLHKVYEYLA QKKILQVLVE
GGTTLHTSLL KERFVNSLVL YSGPMILGDQ KRPLVGVLGN LLESASPLTL KSSQILGNSL
KVVWEISPQV FEPIRN


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