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Database: UniProt/TrEMBL
Entry: C6XXW3_PEDHD
LinkDB: C6XXW3_PEDHD
Original site: C6XXW3_PEDHD 
ID   C6XXW3_PEDHD            Unreviewed;       353 AA.
AC   C6XXW3;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   16-MAR-2016, entry version 47.
DE   RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769};
GN   OrderedLocusNames=Phep_2177 {ECO:0000313|EMBL:ACU04381.1};
OS   Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / NCIB 9290).
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU04381.1, ECO:0000313|Proteomes:UP000000852};
RN   [1] {ECO:0000313|EMBL:ACU04381.1, ECO:0000313|Proteomes:UP000000852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13125 / DSM 2366 / NCIB 9290
RC   {ECO:0000313|Proteomes:UP000000852};
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. {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006769,
CC         ECO:0000256|PIRSR:PIRSR006769-3};
CC       Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769,
CC       ECO:0000256|PIRSR:PIRSR006769-3};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 2/4.
CC       {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 3/4.
CC       {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HTP
CC       reductase family. {ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC       deoxycytidylate deaminase family. {ECO:0000256|PIRNR:PIRNR006769}.
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DR   EMBL; CP001681; ACU04381.1; -; Genomic_DNA.
DR   RefSeq; WP_015807994.1; NZ_AQGK01000001.1.
DR   ProteinModelPortal; C6XXW3; -.
DR   STRING; 485917.Phep_2177; -.
DR   EnsemblBacteria; ACU04381; ACU04381; Phep_2177.
DR   KEGG; phe:Phep_2177; -.
DR   PATRIC; 22881425; VBIPedHep98714_2190.
DR   eggNOG; ENOG4105D1W; Bacteria.
DR   eggNOG; COG0117; LUCA.
DR   eggNOG; COG1985; LUCA.
DR   HOGENOM; HOG000257443; -.
DR   KO; K11752; -.
DR   OMA; WAESADG; -.
DR   OrthoDB; EOG66F07R; -.
DR   BioCyc; PHEP485917:GHL9-2200-MONOMER; -.
DR   UniPathway; UPA00275; UER00401.
DR   Proteomes; UP000000852; Chromosome.
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; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000852};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006769};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006769,
KW   ECO:0000256|PIRSR:PIRSR006769-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-2};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR006769};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000852};
KW   Riboflavin biosynthesis {ECO:0000256|PIRNR:PIRNR006769};
KW   Zinc {ECO:0000256|PIRNR:PIRNR006769, ECO:0000256|PIRSR:PIRSR006769-3}.
FT   DOMAIN        1    131       CMP/dCMP-type deaminase.
FT                                {ECO:0000259|PROSITE:PS51747}.
FT   ACT_SITE     52     52       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006769-1}.
FT   METAL        50     50       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   METAL        83     83       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   METAL        92     92       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   BINDING     162    162       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR006769-
FT                                2}.
FT   BINDING     178    178       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     192    192       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     204    204       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     208    208       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     212    212       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     215    215       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     291    291       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
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
//
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