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Database: UniProt/TrEMBL
Entry: D5URV9_TSUPD
LinkDB: D5URV9_TSUPD
Original site: D5URV9_TSUPD 
ID   D5URV9_TSUPD            Unreviewed;       415 AA.
AC   D5URV9;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   26-NOV-2014, entry version 28.
DE   RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00129533};
GN   Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283};
GN   OrderedLocusNames=Tpau_2561 {ECO:0000313|EMBL:ADG79164.1};
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 {ECO:0000313|EMBL:ADG79164.1, ECO:0000313|Proteomes:UP000001213};
RN   [1] {ECO:0000313|Proteomes:UP000001213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC   {ECO:0000313|Proteomes:UP000001213};
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.
CC       {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00129506}.
CC   -!- FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-
CC       ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and
CC       pyrophosphate. {ECO:0000256|HAMAP-Rule:MF_01283,
CC       ECO:0000256|SAAS:SAAS00129536}.
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4-
CC       dihydroxybutan-2-one 4-phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01283}.
CC   -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = formate + 2,5-diamino-6-
CC       hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine + diphosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- COFACTOR:
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01283};
CC   -!- COFACTOR:
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|HAMAP-Rule:MF_01283};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-
CC       hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step
CC       1/1. {ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-
CC       6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01283}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family. {ECO:0000256|HAMAP-Rule:MF_01283}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP
CC       synthase family. {ECO:0000256|HAMAP-Rule:MF_01283}.
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DR   EMBL; CP001966; ADG79164.1; -; Genomic_DNA.
DR   RefSeq; WP_013127183.1; NC_014158.1.
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   BioCyc; TPAU521096:GI2W-2587-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 {ECO:0000313|Proteomes:UP000001213};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00129530};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000313|EMBL:ADG79164.1};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00129481};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00129540};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001213};
KW   Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283,
KW   ECO:0000256|SAAS:SAAS00129397};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   NP_BIND     257    261       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   NP_BIND     301    303       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   REGION        1    204       DHBP synthase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   REGION       28     29       D-ribulose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   REGION      141    145       D-ribulose 5-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   REGION      205    415       GTP cyclohydrolase II.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   ACT_SITE    335    335       Proton acceptor; for GTP cyclohydrolase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   ACT_SITE    337    337       Nucleophile; for GTP cyclohydrolase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   METAL        29     29       Magnesium or manganese 1.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   METAL        29     29       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   METAL       144    144       Magnesium or manganese 2.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   METAL       262    262       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   METAL       273    273       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   METAL       275    275       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01283}.
FT   BINDING      33     33       D-ribulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     165    165       D-ribulose 5-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     278    278       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     323    323       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     358    358       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   BINDING     363    363       GTP. {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   SITE        127    127       Essential for DHBP synthase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
FT   SITE        165    165       Essential for DHBP synthase activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01283}.
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
//
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