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Database: UniProt/TrEMBL
Entry: C9R9T0_AMMDK
LinkDB: C9R9T0_AMMDK
Original site: C9R9T0_AMMDK 
ID   C9R9T0_AMMDK            Unreviewed;       411 AA.
AC   C9R9T0;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   19-FEB-2014, entry version 28.
DE   RecName: Full=Riboflavin biosynthesis protein RibBA;
GN   Name=ribBA; OrderedLocusNames=Adeg_1980;
OS   Ammonifex degensii (strain DSM 10501 / KC4).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Ammonifex.
OX   NCBI_TaxID=429009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10501 / KC4;
RG   US DOE Joint Genome Institute;
RA   Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA   Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001785; ACX53059.1; -; Genomic_DNA.
DR   RefSeq; YP_003239909.1; NC_013385.1.
DR   STRING; 429009.Adeg_1980; -.
DR   EnsemblBacteria; ACX53059; ACX53059; Adeg_1980.
DR   GeneID; 8491987; -.
DR   KEGG; adg:Adeg_1980; -.
DR   PATRIC; 20883544; VBIAmmDeg104956_1977.
DR   eggNOG; COG0108; -.
DR   HOGENOM; HOG000115440; -.
DR   KO; K14652; -.
DR   OrthoDB; EOG679TK8; -.
DR   BioCyc; ADEG429009:GHG1-2030-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     252    256       GTP (By similarity).
FT   NP_BIND     295    297       GTP (By similarity).
FT   REGION        1    201       DHBP synthase (By similarity).
FT   REGION       28     29       D-ribulose 5-phosphate binding (By
FT                                similarity).
FT   REGION      140    144       D-ribulose 5-phosphate binding (By
FT                                similarity).
FT   REGION      202    411       GTP cyclohydrolase II (By similarity).
FT   ACT_SITE    329    329       Proton acceptor; for GTP cyclohydrolase
FT                                activity (By similarity).
FT   ACT_SITE    331    331       Nucleophile; for GTP cyclohydrolase
FT                                activity (By similarity).
FT   METAL        29     29       Magnesium or manganese 1 (By similarity).
FT   METAL        29     29       Magnesium or manganese 2 (By similarity).
FT   METAL       143    143       Magnesium or manganese 2 (By similarity).
FT   METAL       257    257       Zinc; catalytic (By similarity).
FT   METAL       268    268       Zinc; catalytic (By similarity).
FT   METAL       270    270       Zinc; catalytic (By similarity).
FT   BINDING      33     33       D-ribulose 5-phosphate (By similarity).
FT   BINDING     164    164       D-ribulose 5-phosphate (By similarity).
FT   BINDING     273    273       GTP (By similarity).
FT   BINDING     317    317       GTP (By similarity).
FT   BINDING     352    352       GTP (By similarity).
FT   BINDING     357    357       GTP (By similarity).
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   411 AA;  45241 MW;  94FCFF0C0335EB71 CRC64;
     MFKFNTVEEA IADIREGKMV IVVDDEDREN EGDLVMAAEK VTPEAITFMA TYGRGLICVP
     LTEERADELD LAPMVPYNTD PHGTAFTVSV DARGVTTGIS AHERAYTIKK LIDPKAGPHD
     FRRPGHVFPL RAKKGGVLRR AGHTEAAVDL ARLAGLYPAG VICEIMKDDG TMARVPELME
     FARRHNLKII TIADLISYRR RTEKLVRRVG AARLPTKYGE FTAVAYESLL DGKGHLALVM
     GDLSSVEAPL VRVHSECLTG DVFGSLRCDC GQQIERALRM IAAEGVGVLL YMRQEGRGIG
     LLNKIRAYEL QDRGKDTVEA NEALGFPPDL RDYGIGAQIL VDLGLKKIRL LTNNPRKIKG
     IQGYGLEIVE RVPLEVPPGK ENGFYLATKK KKLGHLLTLV DQQEEGSKSN A
//
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