ID C6XXW3_PEDHD Unreviewed; 353 AA.
AC C6XXW3;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 28.
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 DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Glavina del Rio T., Tice H.,
RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Mikhailova N.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.C., Saunders E., Chertkov O., Brettin T., Goeker M.,
RA Rohde M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N., 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 -!- COFACTOR: Binds 1 zinc ion (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC 6-(D-ribitylamino)uracil from GTP.
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; WYGRNPV; -.
DR BioCyc; PHEP485917:GHL9-2199-MONOMER; -.
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-KW.
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; SSF53927; Cytidine_deaminase-like; 1.
DR SUPFAM; SSF53597; SSF53597; 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
//
