(data stored in ACNUC7421 zone)

SWISSPROT: D4YXP3_SPHJU

ID   D4YXP3_SPHJU            Unreviewed;       317 AA.
AC   D4YXP3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 41.
DE   SubName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase {ECO:0000313|EMBL:BAI95125.1};
DE            EC=1.1.1.193 {ECO:0000313|EMBL:BAI95125.1};
DE            EC=3.5.4.26 {ECO:0000313|EMBL:BAI95125.1};
GN   Name=ribD {ECO:0000313|EMBL:BAI95125.1};
GN   OrderedLocusNames=SJA_C1-02910 {ECO:0000313|EMBL:BAI95125.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95125.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95125.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006769-3};
CC       Note=Binds 1 zinc ion. {ECO:0000256|PIRSR:PIRSR006769-3};
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DR   EMBL; AP010803; BAI95125.1; -; Genomic_DNA.
DR   RefSeq; WP_013038921.1; NC_014006.1.
DR   ProteinModelPortal; D4YXP3; -.
DR   STRING; 452662.SJA_C1-02910; -.
DR   EnsemblBacteria; BAI95125; BAI95125; SJA_C1-02910.
DR   GeneID; 29271994; -.
DR   KEGG; sjp:SJA_C1-02910; -.
DR   eggNOG; ENOG4105D1W; Bacteria.
DR   eggNOG; COG0117; LUCA.
DR   HOGENOM; HOG000257442; -.
DR   KO; K11752; -.
DR   OMA; DEMYMAR; -.
DR   OrthoDB; POG091H01D3; -.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.430.10; -; 2.
DR   InterPro; IPR002125; CMP_dCMP_dom.
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; 2.
DR   PIRSF; PIRSF006769; RibD; 2.
DR   SUPFAM; SSF53597; SSF53597; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR00326; eubact_ribD; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   4: Predicted;
DR   PRODOM; D4YXP3.
DR   SWISS-2DPAGE; D4YXP3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Hydrolase {ECO:0000313|EMBL:BAI95125.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006769-3};
KW   NADP {ECO:0000256|PIRSR:PIRSR006769-2};
KW   Oxidoreductase {ECO:0000313|EMBL:BAI95125.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006769-3}.
FT   DOMAIN        1    118       CMP/dCMP-type deaminase.
FT                                {ECO:0000259|PROSITE:PS51747}.
FT   NP_BIND     248    254       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   ACT_SITE     46     46       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006769-1}.
FT   METAL        44     44       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   METAL        69     69       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   METAL        79     79       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR006769-3}.
FT   BINDING     149    149       NADP; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR006769-
FT                                2}.
FT   BINDING     163    163       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     165    165       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     179    179       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     191    191       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     195    195       NADP. {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     199    199       Substrate; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR006769-2}.
FT   BINDING     202    202       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
FT   BINDING     246    246       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR006769-2}.
SQ   SEQUENCE   317 AA;  33741 MW;  A8F92C526C7BDECB CRC64;
     MAAAIALSQR GRGLSTPNPN VGCLIVKDGH VVGRGWTQRG GRPHAEAQAL DEALDRARGA
     TAYVTLEPCF HLSPRGPRCA DRMARAGVRR VVIALRDPDP RTDGQGAAWL RQHGVAVDMG
     LMAGEAAAAM RGFVLRQTLG RPAVTLKLGL SLDGRIALAD GSSRWITGPE ARAHAHMERA
     RHDAILVGGG TLRADAPRLD VRLLGLEDRS PRRVLLSHGD APGGWETIAA PEDIAALPQV
     DHLLVEGGAQ AAAAFLRADL VDRLLLYRAP ILIGAGLAGV GDIGLTDLAG AHGRWRLDDE
     RRLGNDRLEV YLRSRNA
//

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