ID E8RDT3_DESPD Unreviewed; 414 AA.
AC E8RDT3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 01-MAY-2013, entry version 20.
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; LRCDCRM; -.
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:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
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 253 257 GTP (By similarity).
FT NP_BIND 296 298 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 202 414 GTP cyclohydrolase II (By similarity).
FT ACT_SITE 331 331 Proton acceptor; for GTP cyclohydrolase
FT activity (By similarity).
FT ACT_SITE 333 333 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 258 258 Zinc; catalytic (By similarity).
FT METAL 269 269 Zinc; catalytic (By similarity).
FT METAL 271 271 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 274 274 GTP (By similarity).
FT BINDING 319 319 GTP (By similarity).
FT BINDING 354 354 GTP (By similarity).
FT BINDING 359 359 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 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
//
