ID   C6XXW3_PEDHD            Unreviewed;       353 AA.
AC   C6XXW3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   14-MAY-2014, entry version 33.
DE   RecName: Full=Riboflavin biosynthesis protein RibD;
GN   OrderedLocusNames=Phep_2177;
OS   Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290).
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=485917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290;
RX   PubMed=21304637; DOI=10.4056/sigs.22138;
RA   Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA   Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA   Pitluck S., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goker M.,
RA   Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Pedobacter heparinus type strain (HIM
RT   762-3).";
RL   Stand. Genomic Sci. 1:54-62(2009).
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 (By similarity).
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-phospho-D-ribitylamino)uracil +
CC       NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH.
CC   -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 2/4.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 3/4.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HTP
CC       reductase family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC       deoxycytidylate deaminase family.
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DR   EMBL; CP001681; ACU04381.1; -; Genomic_DNA.
DR   RefSeq; YP_003092443.1; NC_013061.1.
DR   ProteinModelPortal; C6XXW3; -.
DR   STRING; 485917.Phep_2177; -.
DR   EnsemblBacteria; ACU04381; ACU04381; Phep_2177.
DR   GeneID; 8253283; -.
DR   KEGG; phe:Phep_2177; -.
DR   PATRIC; 22881425; VBIPedHep98714_2190.
DR   eggNOG; COG0117; -.
DR   HOGENOM; HOG000257443; -.
DR   KO; K11752; -.
DR   OMA; IILKWAE; -.
DR   OrthoDB; EOG66F07R; -.
DR   BioCyc; PHEP485917:GHL9-2200-MONOMER; -.
DR   UniPathway; UPA00275; UER00401.
DR   GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:InterPro.
DR   GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.430.10; -; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_Zn-bd.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR024072; DHFR-like_dom.
DR   InterPro; IPR004794; Eubact_RibD.
DR   InterPro; IPR002734; RibDG_C.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   Pfam; PF01872; RibD_C; 1.
DR   PIRSF; PIRSF006769; RibD; 1.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00326; eubact_ribD; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Metal-binding; NADP; Oxidoreductase;
KW   Riboflavin biosynthesis; Zinc.
SQ   SEQUENCE   353 AA;  39465 MW;  131FBE71AB265435 CRC64;
     MTNELYMQRC LELAAMGMGN VSPNPMVGCV IVSDGKIIGE GYHARFGEAH AEVNAINSVV
     HNYGNTAETL LAAATAYVSL EPCAHFGKTP PCADLLIKHR IKKVVIGNTD PFDGVNGKGI
     EKLKNAGIEV VSGVLEAECS QLNRRFFTRI GQQHPYIILK WATSANGYFA PENTTQQWIS
     GPEAKKLVHK WRTEEDAVLV GRLTAMADNP RLTVREWYGR NPVRIVVDRH LQVPSSHHIY
     NKEAKTIIFN EQKTDVQENI HFIQMEDMQH YLPQKIAFQL YLMDIASVII EGGAQVLNQF
     IQARLWDEAR VFRSAVSWPA GIPSPELNLQ SCAITDQFPI GKDQLTIYKN NPS
//