ID C9R9T0_AMMDK Unreviewed; 411 AA.
AC C9R9T0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 01-MAY-2013, entry version 24.
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 BioCyc; ADEG429009:GHG1-2058-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 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
//
