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 23-FEB-2022, entry version 75. 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}; OrderedLocusNames=MMAR_2222; OS Mycobacterium marinum (strain ATCC BAA-535 / M). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC 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., Churcher C., RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A., RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.; RT "Insights from the complete genome sequence of Mycobacterium marinum on the RT evolution of Mycobacterium tuberculosis."; RL Genome Res. 18:729-741(2008). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate CC and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000255|HAMAP- CC 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: CC Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + CC formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830; CC EC=4.1.99.12; Evidence={ECO:0000255|HAMAP-Rule:MF_01283}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)- CC pyrimidine + formate + 3 H(+) + 2 phosphate; Xref=Rhea:RHEA:23704, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58614; EC=3.5.4.25; CC Evidence={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-Rule:MF_01283}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3- CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01283}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC 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 synthase CC 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; WP_012393985.1; NC_010612.1. DR SMR; B2HP67; -. DR STRING; 216594.MMAR_2222; -. DR PRIDE; B2HP67; -. DR EnsemblBacteria; ACC40671; ACC40671; MMAR_2222. DR GeneID; 64260907; -. DR KEGG; mmi:MMAR_2222; -. DR eggNOG; COG0108; Bacteria. DR eggNOG; COG0807; Bacteria. DR HOGENOM; CLU_020273_1_2_11; -. DR OMA; ECRGLIC; -. DR OrthoDB; 900513at2; -. 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-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd00641; GTP_cyclohydro2; 1. DR Gene3D; 3.40.50.10990; -; 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; IPR032677; GTP_cyclohydro_II. DR InterPro; IPR000926; RibA. DR InterPro; IPR036144; RibA-like_sf. DR InterPro; IPR016299; Riboflavin_synth_RibBA. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF142695; SSF142695; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00505; ribA; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 3: Inferred from homology; KW GTP-binding; Hydrolase; Lyase; Magnesium; Manganese; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Reference proteome; KW Riboflavin biosynthesis; Zinc. FT CHAIN 1..425 FT /note="Riboflavin biosynthesis protein RibBA" FT /id="PRO_1000140366" FT NP_BIND 259..263 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT NP_BIND 303..305 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT REGION 1..204 FT /note="DHBP synthase" FT REGION 28..29 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT REGION 141..145 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT REGION 205..425 FT /note="GTP cyclohydrolase II" FT ACT_SITE 337 FT /note="Proton acceptor; for GTP cyclohydrolase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT ACT_SITE 339 FT /note="Nucleophile; for GTP cyclohydrolase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT METAL 29 FT /note="Magnesium or manganese 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT METAL 29 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT METAL 144 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT METAL 264 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT METAL 275 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT METAL 277 FT /note="Zinc; catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT BINDING 33 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT BINDING 165 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT BINDING 280 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT BINDING 325 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT BINDING 360 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT BINDING 365 FT /note="GTP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT SITE 127 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01283" FT SITE 165 FT /note="Essential for DHBP synthase activity" FT /evidence="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 //