ID   RIBD_CHLMU              Reviewed;         371 AA.
AC   Q9PLJ6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Riboflavin biosynthesis protein ribD;
DE   Includes:
DE     RecName: Full=Diaminohydroxyphosphoribosylaminopyrimidine deaminase;
DE              Short=DRAP deaminase;
DE              EC=3.5.4.26;
DE     AltName: Full=Riboflavin-specific deaminase;
DE   Includes:
DE     RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase;
DE              EC=1.1.1.193;
DE     AltName: Full=HTP reductase;
GN   Name=ribD; OrderedLocusNames=TC_0103;
OS   Chlamydia muridarum.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=83560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
CC   -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone
CC       5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-
CC       pyrimidinedione 5'-phosphate.
CC   -!- CATALYTIC ACTIVITY: 2,5-diamino-6-hydroxy-4-(5-
CC       phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5-
CC       phosphoribosylamino)uracil + NH(3).
CC   -!- CATALYTIC ACTIVITY: 5-amino-6-(5-phosphoribitylamino)uracil +
CC       NADP(+) = 5-amino-6-(5-phosphoribosylamino)uracil + NADPH.
CC   -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 6,7-
CC       dimethyl-8-(1-D-ribityl)lumazine from GTP: step 2/4.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 6,7-
CC       dimethyl-8-(1-D-ribityl)lumazine from GTP: step 3/4.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC       deoxycytidylate deaminases family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HTP
CC       reductase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE002160; AAF38983.1; ALT_INIT; Genomic_DNA.
DR   PIR; D81742; D81742.
DR   RefSeq; NP_296487.1; -.
DR   GeneID; 1245633; -.
DR   GenomeReviews; AE002160_GR; TC_0103.
DR   KEGG; cmu:TC0103; -.
DR   TIGR; TC_0103; -.
DR   HOGENOM; Q9PLJ6; -.
DR   BioCyc; CMUR243161:TC_0103-MON; -.
DR   BRENDA; 1.1.1.193; 256349.
DR   BRENDA; 3.5.4.26; 256349.
DR   GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil red...; IEA:EC.
DR   GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine...; IEA:EC.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_Zn_bd.
DR   InterPro; IPR004794; Eubact_ribD.
DR   InterPro; IPR011549; RibD_C.
DR   InterPro; IPR002734; RibDG_C.
DR   PANTHER; PTHR11079:SF10; Eubact_ribD; 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   Pfam; PF01872; RibD_C; 1.
DR   TIGRFAMs; TIGR00326; eubact_ribD; 1.
DR   TIGRFAMs; TIGR00227; ribD_Cterm; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; Multifunctional enzyme;
KW   NADP; Oxidoreductase; Riboflavin biosynthesis; Zinc.
FT   CHAIN         1    371       Riboflavin biosynthesis protein ribD.
FT                                /FTId=PRO_0000171717.
FT   NP_BIND     301    307       NADP (By similarity).
FT   REGION        1    150       Deaminase.
FT   REGION      151    371       Reductase.
FT   ACT_SITE     57     57       Proton donor (By similarity).
FT   METAL        55     55       Zinc; catalytic (By similarity).
FT   METAL        80     80       Zinc; catalytic (By similarity).
FT   METAL        89     89       Zinc; catalytic (By similarity).
FT   BINDING     159    159       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     173    173       Substrate (By similarity).
FT   BINDING     175    175       NADP (By similarity).
FT   BINDING     189    189       Substrate (By similarity).
FT   BINDING     201    201       NADP (By similarity).
FT   BINDING     205    205       NADP (By similarity).
FT   BINDING     209    209       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     212    212       Substrate (By similarity).
FT   BINDING     230    230       NADP (By similarity).
FT   BINDING     299    299       Substrate (By similarity).
SQ   SEQUENCE   371 AA;  40912 MW;  2A37C047D233A1CA CRC64;
     MEVSSEQQLF FMREAVALGE RGRIFAPPNP WVGCVIVKNG CIIGRGWHKG IGSPHAEVCA
     FQDQTSSLVG ADVYVTLEPC CHFGRTPPCV DLLIKSKVSS VYIALLDPDP RVCKRGVARL
     KEAGISVYVG IGHEEAKASL QPYLHQRETG LPWVVMKTAA SLDGQTSDRR GISQWISGEQ
     ARLDVGRLRA ESQAVIVGSR TVCLDNPRLS ARMPSGDLYE RQPLRVVVDS RGSVPLDARV
     WNPDSGNVLL ATTEQCSKEH IQKLEDRGVE VWKSSPQQVD LKRLLQYLAE KGCLQVLVEG
     GARLHSAFWR EHLVNAGVIY WGPKFLGDQG SPMLRDLQLC LDNAEHVKIT KTFLVGDSVK
     TCFECVGRED G
//