ID RIBBA_MYCMM Reviewed; 425 AA. AC B2HP67; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 07-JAN-2015, entry version 47. DE RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000255|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01283}; DE Short=DHBP synthase {ECO:0000255|HAMAP-Rule:MF_01283}; DE EC=4.1.99.12 {ECO:0000255|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000255|HAMAP-Rule:MF_01283}; DE EC=3.5.4.25 {ECO:0000255|HAMAP-Rule:MF_01283}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000255|HAMAP-Rule:MF_01283}; GN Name=ribBA {ECO:0000255|HAMAP-Rule:MF_01283}; GN OrderedLocusNames=MMAR_2222; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=216594; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-535 / M; RX PubMed=18403782; DOI=10.1101/gr.075069.107; RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., RA Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., RA Jagels K., Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A., RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., RA Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.; RT "Insights from the complete genome sequence of Mycobacterium marinum RT on the evolution of Mycobacterium tuberculosis."; RL Genome Res. 18:729-741(2008). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to CC formate and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01283}. 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:0000255|HAMAP-Rule:MF_01283}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01283}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01283}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01283}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000255|HAMAP-Rule:MF_01283}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01283}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC 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:0000255|HAMAP-Rule:MF_01283}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. {ECO:0000255|HAMAP- CC Rule:MF_01283}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000255|HAMAP-Rule:MF_01283}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000255|HAMAP-Rule:MF_01283}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000854; ACC40671.1; -; Genomic_DNA. DR RefSeq; YP_001850526.1; NC_010612.1. DR STRING; 216594.MMAR_2222; -. DR EnsemblBacteria; ACC40671; ACC40671; MMAR_2222. DR GeneID; 6226486; -. DR KEGG; mmi:MMAR_2222; -. DR PATRIC; 18065383; VBIMycMar75906_2373. DR eggNOG; COG0108; -. DR HOGENOM; HOG000115440; -. DR KO; K14652; -. DR OMA; LMVDRNT; -. DR OrthoDB; EOG679TK8; -. DR BioCyc; MMAR216594:GJOB-2237-MONOMER; -. DR UniPathway; UPA00275; UER00399. DR UniPathway; UPA00275; UER00400. DR Proteomes; UP000001190; Chromosome. 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; GTP-binding; Hydrolase; Lyase; Magnesium; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Reference proteome; Riboflavin biosynthesis; Zinc. FT CHAIN 1 425 Riboflavin biosynthesis protein RibBA. FT /FTId=PRO_1000140366. FT NP_BIND 259 263 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT NP_BIND 303 305 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT REGION 1 204 DHBP synthase. FT REGION 28 29 D-ribulose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT REGION 141 145 D-ribulose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT REGION 205 425 GTP cyclohydrolase II. FT ACT_SITE 337 337 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT ACT_SITE 339 339 Nucleophile; for GTP cyclohydrolase FT activity. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT METAL 29 29 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT METAL 29 29 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT METAL 144 144 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT METAL 264 264 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT METAL 275 275 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT METAL 277 277 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01283}. FT BINDING 33 33 D-ribulose 5-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 165 165 D-ribulose 5-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 280 280 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 325 325 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 360 360 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT BINDING 365 365 GTP. {ECO:0000255|HAMAP-Rule:MF_01283}. FT SITE 127 127 Essential for DHBP synthase activity. FT {ECO:0000255|HAMAP-Rule:MF_01283}. FT SITE 165 165 Essential for DHBP synthase activity. FT {ECO:0000255|HAMAP-Rule:MF_01283}. SQ SEQUENCE 425 AA; 46040 MW; F215B0743502C0EA CRC64; MTRLDSVERA VADIGAGKAV IVIDDEDREN EGDLIFAAEK ATPELVAFMV RYTSGYLCVP LDGAVCDRLG LLPMYAVNQD KHGTAYTVTV DAKNGVGTGI SASDRATTMR LLADPASVAE DFTRPGHVVP LRAKDGGVLR RPGHTEAAVD LARMAGLQPA GAICEIVSQK DEGSMAQTDE LRVFADEHGL ALITIADLIE WRRKHEKHIE RVAEARIPTR HGEFRAIGYT SIYEDVEHVA LVRGEIAGPN SDGDDVLVRV HSECLTGDVF GSRRCDCGPQ LDAAMAMVAR EGRGVVLYMR GHEGRGIGLL HKLQAYQLQD AGDDTVDANL KLGLPADARD YGIGAQILVD LGVRSMRLLT NNPAKRVGLD GYGLHIIERV PLPVRANAEN IRYLMTKRDR MGHDLTGLDD FHESVHLPGE FGGAL //