GenomeNet

Database: UniProt/TrEMBL
Entry: B9M1E5_GEOSF
LinkDB: B9M1E5_GEOSF
Original site: B9M1E5_GEOSF 
ID   B9M1E5_GEOSF            Unreviewed;       400 AA.
AC   B9M1E5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   01-MAY-2013, entry version 36.
DE   RecName: Full=Riboflavin biosynthesis protein RibBA;
GN   Name=ribBA; OrderedLocusNames=Geob_2677;
OS   Geobacter sp. (strain FRC-32).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=316067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRC-32;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001390; ACM21027.1; -; Genomic_DNA.
DR   RefSeq; YP_002538128.1; NC_011979.1.
DR   ProteinModelPortal; B9M1E5; -.
DR   SMR; B9M1E5; 3-203, 206-376.
DR   STRING; 316067.Geob_2677; -.
DR   EnsemblBacteria; ACM21027; ACM21027; Geob_2677.
DR   GeneID; 7361332; -.
DR   KEGG; geo:Geob_2677; -.
DR   PATRIC; 22012021; VBIGeoSp137169_2768.
DR   eggNOG; COG0108; -.
DR   HOGENOM; HOG000115440; -.
DR   KO; K14652; -.
DR   OMA; LRCDCRM; -.
DR   ProtClustDB; CLSK828487; -.
DR   BioCyc; GSP316067:GHSV-2708-MONOMER; -.
DR   UniPathway; UPA00275; UER00399.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
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; DHBP_synth_RibB-like_a/b_dom; 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       27     28       D-ribulose 5-phosphate binding (By
FT                                similarity).
FT   REGION      202    400       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        28     28       Magnesium or manganese 1 (By similarity).
FT   METAL        28     28       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      32     32       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   400 AA;  43536 MW;  78FDC869BFE9DB04 CRC64;
     MTVAKIEDAI EDIRQGKMVI LVDDEDRENE GDLTMAAEKV TPEAINFMAK YGRGLICLTL
     TGDKCDQLNL PPMVSTNTSS FGTAFTVSIE AKKGVTTGIS AADRAHTILT AVADDASADD
     LARPGHVFPL RAKAGGVLVR AGQTEGSVDL ARLAGLKHAG VICEIMNDDG TMSRMPELKK
     FAKEHGIKVC TIADLVAYRL KHESLVRRAA EVRLPSQLGE FSAIAFENDI DKLEHLALVK
     GEIRGDEPVL VRVHSECLTG DVFASIRCDC AEQLHRAMEM VEAEGKGVVL YMRQEGRGIG
     LINKLKAYAL QDQGKDTVEA NLALGFKADL RDYGIGAQIL VNLGIKNIRL MTNNPKKIVG
     LEGYGINIVE RVPIEIAPSM SNKKYLKTKR EKMGHLLENI
//
DBGET integrated database retrieval system