ID A0A1W1VHZ1_DESTI Unreviewed; 398 AA. AC A0A1W1VHZ1; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 25-MAY-2022, entry version 27. DE RecName: Full=Riboflavin biosynthesis protein RibBA {ECO:0000256|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01283}; DE Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_01283}; DE EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_01283}; DE Includes: DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_01283}; DE EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_01283}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_01283}; GN Name=ribBA {ECO:0000256|HAMAP-Rule:MF_01283}; GN ORFNames=SAMN00017405_2111 {ECO:0000313|EMBL:SMB92840.1}; OS Desulfonispora thiosulfatigenes DSM 11270. OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae; OC Desulfonispora. OX NCBI_TaxID=656914 {ECO:0000313|EMBL:SMB92840.1, ECO:0000313|Proteomes:UP000192731}; RN [1] {ECO:0000313|EMBL:SMB92840.1, ECO:0000313|Proteomes:UP000192731} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11270 {ECO:0000313|EMBL:SMB92840.1, RC ECO:0000313|Proteomes:UP000192731}; RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I., RA Dimitrov K.M., Suarez D.L., Swayne D.E.; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate CC and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000256|ARBA:ARBA00002284, ECO:0000256|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:0000256|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:0000256|ARBA:ARBA00000141, CC ECO:0000256|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:0000256|ARBA:ARBA00029293, ECO:0000256|HAMAP- CC Rule:MF_01283}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000256|HAMAP-Rule:MF_01283}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|ARBA:ARBA00004904, ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D- CC ribitylamino)uracil from GTP: step 1/4. {ECO:0000256|ARBA:ARBA00004853, CC ECO:0000256|HAMAP-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 synthase CC family. {ECO:0000256|ARBA:ARBA00005520, ECO:0000256|HAMAP- CC 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; FWWT01000021; SMB92840.1; -; Genomic_DNA. DR STRING; 656914.SAMN00017405_2111; -. DR EnsemblBacteria; SMB92840; SMB92840; SAMN00017405_2111. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000192731; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01283}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01283}; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01283}; Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01283}; Reference proteome {ECO:0000313|Proteomes:UP000192731}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_01283}; Zinc {ECO:0000256|HAMAP-Rule:MF_01283}. FT DOMAIN 210..372 FT /note="GTP_cyclohydro2" FT /evidence="ECO:0000259|Pfam:PF00925" FT NP_BIND 251..255 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT NP_BIND 294..296 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 1..200 FT /note="DHBP synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 27..28 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 139..143 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 201..398 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 328 FT /note="Proton acceptor; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 330 FT /note="Nucleophile; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 28 FT /note="Magnesium or manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 28 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 142 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 256 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 267 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 269 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 32 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 163 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 272 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 316 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 351 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 356 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 125 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 163 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" SQ SEQUENCE 398 AA; 44311 MW; A847D91FDEDEF327 CRC64; MKFDLIEEAI EDIRQGKMLI VVDDEDRENE GDLVIAADKV TPEAINFMAS YGKGLVCLPI IGERLDELEI SPMVNKNTDN LGTAFTVSID AKETTTGISA FERSLTIQKV LEEGVKPEDF KRPGHIFPLR YQEGGVLKRT GHTEAAVDLA RLADCYPAGV ICEIMSEDGT MARVPELMEF SKKHGIKIIT IADLIKYRRN TEKLIKKVGK TNMPTKYGDF ELHAYEETLT GVTHVALVRG DVNTEDPVLV RVHSQCLTGD VLGSLRCDCG NQLEQALKNI ISENRGVFLY MSQEGRGIGL ANKIRAYILQ DQGIDTVEAN EMLGFPADLR DYGTGAQILV DLGIKNIKLM TNNPRKIRGL EGHGLKIVKR VPIEIKPVIY NKRYLNTKKD KLGHLICK //