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Database: UniProt/TrEMBL
Entry: E8RDT3_DESPD
LinkDB: E8RDT3_DESPD
Original site: E8RDT3_DESPD 
ID   E8RDT3_DESPD            Unreviewed;       414 AA.
AC   E8RDT3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   11-JUN-2014, entry version 25.
DE   RecName: Full=Riboflavin biosynthesis protein RibBA;
GN   Name=ribBA; OrderedLocusNames=Despr_0767;
OS   Desulfobulbus propionicus (strain ATCC 33891 / DSM 2032 / 1pr3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfobulbus.
OX   NCBI_TaxID=577650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33891 / DSM 2032 / 1pr3;
RX   PubMed=21475592;
RA   Pagani I., Lapidus A., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Chertkov O., Davenport K., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Mavromatis K., Ivanova N., Mikhailova N.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brambilla E., Kannan K.P., Djao O.D.,
RA   Rohde M., Pukall R., Spring S., Goker M., Sikorski J., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Desulfobulbus propionicus type strain
RT   (1pr3).";
RL   Stand. Genomic Sci. 4:100-110(2011).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to
CC       formate and 3,4-dihydroxy-2-butanone 4-phosphate (By similarity).
CC   -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC       ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC       pyrophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC       dihydroxybutan-2-one 4-phosphate.
CC   -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
CC       hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
CC       hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
CC       1/1.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 1/4.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP
CC       synthase family.
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DR   EMBL; CP002364; ADW16941.1; -; Genomic_DNA.
DR   RefSeq; YP_004194232.1; NC_014972.1.
DR   EnsemblBacteria; ADW16941; ADW16941; Despr_0767.
DR   GeneID; 10173479; -.
DR   KEGG; dpr:Despr_0767; -.
DR   PATRIC; 46934950; VBIDesPro114934_0812.
DR   HOGENOM; HOG000115440; -.
DR   KO; K14652; -.
DR   OMA; GKGLICM; -.
DR   BioCyc; DPRO577650:GH80-780-MONOMER; -.
DR   UniPathway; UPA00275; UER00399.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.870.10; -; 1.
DR   HAMAP; MF_00179; RibA; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   HAMAP; MF_01283; RibBA; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   InterPro; IPR000926; GTP_CycHdrlaseII_RibA.
DR   InterPro; IPR016299; Riboflavin_synth_RibBA.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   PIRSF; PIRSF001259; RibA; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00505; ribA; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
KW   Complete proteome; GTP-binding; Hydrolase; Lyase; Magnesium;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Riboflavin biosynthesis; Zinc.
FT   NP_BIND     253    257       GTP (By similarity){EA2}.
FT   NP_BIND     296    298       GTP (By similarity){EA2}.
FT   REGION        1    201       DHBP synthase (By similarity).
FT   REGION       27     28       D-ribulose 5-phosphate binding (By
FT                                similarity).
FT   REGION      202    414       GTP cyclohydrolase II (By similarity).
FT   ACT_SITE    331    331       Proton acceptor; for GTP cyclohydrolase
FT                                activity (By similarity){EA2}.
FT   ACT_SITE    333    333       Nucleophile; for GTP cyclohydrolase
FT                                activity (By similarity){EA2}.
FT   METAL        28     28       Magnesium or manganese 1 (By
FT                                similarity){EA2}.
FT   METAL        28     28       Magnesium or manganese 2 (By
FT                                similarity){EA2}.
FT   METAL       258    258       Zinc; catalytic (By similarity){EA2}.
FT   METAL       269    269       Zinc; catalytic (By similarity){EA2}.
FT   METAL       271    271       Zinc; catalytic (By similarity){EA2}.
FT   BINDING      32     32       D-ribulose 5-phosphate (By
FT                                similarity){EA2}.
FT   BINDING     164    164       D-ribulose 5-phosphate (By
FT                                similarity){EA2}.
FT   BINDING     274    274       GTP (By similarity){EA2}.
FT   BINDING     319    319       GTP (By similarity){EA2}.
FT   BINDING     354    354       GTP (By similarity){EA2}.
FT   BINDING     359    359       GTP (By similarity){EA2}.
FT   SITE        126    126       Essential for DHBP synthase activity (By
FT                                similarity).
FT   SITE        164    164       Essential for DHBP synthase activity (By
FT                                similarity).
SQ   SEQUENCE   414 AA;  45370 MW;  930BF8E38B71FA66 CRC64;
     MAVSSIEEVV EDIKAGKMVI LVDDEDRENE GDLCMAAELV TPEAINFMAT HGRGLICLAL
     SPDIVDQLGL PMMVSNNQSP YGTGFTISIE ARTGVSTGIS AADRARTIEA AVHPKATPRD
     IISPGHIFPL RARGGGVLVR TGQTEGSVDL ARIAGLRTAG IICEIMKDDG TMARMPDLEI
     FAEQHGLKIA TIADLVAYRL RKDVLVRRAA EARLPTYHAG EFRLIAYQND VDKQEHVALV
     KGEINPDEPV MVRVHSECLT GDVFGSARCD CGSQLHAAMR MVEQEGKGVV LYMRQEGRGI
     GLINKLKAYK LQDNDGLDTV EANIRLGFKP DLRDYGIGAQ ILRDLGVRKM RLLTNNPKKI
     IGLEGYGLEV VDRLPIEIPG DEENKDYLRT KRDKMGHILE LYGDMPMGCV TRDP
//
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