ID D5URV9_TSUPD Unreviewed; 415 AA.
AC D5URV9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 01-MAY-2013, entry version 21.
DE RecName: Full=Riboflavin biosynthesis protein RibBA;
GN Name=ribBA; OrderedLocusNames=Tpau_2561;
OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Tsukamurellaceae; Tsukamurella.
OX NCBI_TaxID=521096;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL Submitted (MAR-2010) 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; CP001966; ADG79164.1; -; Genomic_DNA.
DR RefSeq; YP_003647503.1; NC_014158.1.
DR EnsemblBacteria; ADG79164; ADG79164; Tpau_2561.
DR GeneID; 9156722; -.
DR KEGG; tpr:Tpau_2561; -.
DR PATRIC; 38308431; VBITsuPau718_2561.
DR HOGENOM; HOG000115440; -.
DR KO; K14652; -.
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 257 261 GTP (By similarity).
FT NP_BIND 301 303 GTP (By similarity).
FT REGION 1 204 DHBP synthase (By similarity).
FT REGION 28 29 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 141 145 D-ribulose 5-phosphate binding (By
FT similarity).
FT REGION 205 415 GTP cyclohydrolase II (By similarity).
FT ACT_SITE 335 335 Proton acceptor; for GTP cyclohydrolase
FT activity (By similarity).
FT ACT_SITE 337 337 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 144 144 Magnesium or manganese 2 (By similarity).
FT METAL 262 262 Zinc; catalytic (By similarity).
FT METAL 273 273 Zinc; catalytic (By similarity).
FT METAL 275 275 Zinc; catalytic (By similarity).
FT BINDING 33 33 D-ribulose 5-phosphate (By similarity).
FT BINDING 165 165 D-ribulose 5-phosphate (By similarity).
FT BINDING 278 278 GTP (By similarity).
FT BINDING 323 323 GTP (By similarity).
FT BINDING 358 358 GTP (By similarity).
FT BINDING 363 363 GTP (By similarity).
FT SITE 127 127 Essential for DHBP synthase activity (By
FT similarity).
FT SITE 165 165 Essential for DHBP synthase activity (By
FT similarity).
SQ SEQUENCE 415 AA; 44515 MW; 0C74C151BEB9177D CRC64;
MTRFDSIERA IEDIAAGKAV VVVDDEDREN EGDLIFAAEK ATPELVAFMV RYTSGYLCVP
LDGATCDKLG LPPMYATNQD KHGTAYTVTV DAKAGVGTGI SAADRATTML KLADPDSTVD
DFTRPGHVVP LRAKEGGVLR RPGHTEAAVD LATMAGLAPA GVICEIVSEK DPGGMAQTDE
LRVFADDHDL ALISIADLIA WRRKHEKHVV QVASARIPTA HGDFQAVGYT SIHDDVEHVA
LVKGDITADG GADVLVRVHS ECLTGDVFGS LRCDCGPQLD AAMEMVAQEG RGVVLYMRGH
EGRGIGLMHK LQAYQLQDGG ADTVDANLQL GLPADARDYG LGAQILVDLG ITSMRLLTNN
PAKRVGLDGY GLQITERVPM PLRANAENIH YLRTKRDRMG HDMRDLDHFD QGGTA
//
