ID D1CIT3_THET1 Unreviewed; 407 AA. AC D1CIT3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 13-SEP-2023, entry version 95. 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 OrderedLocusNames=Tter_2767 {ECO:0000313|EMBL:ACZ43653.1}; OS Thermobaculum terrenum (strain ATCC BAA-798 / YNP1). OC Bacteria; Chloroflexota; Thermobaculum. OX NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ43653.1, ECO:0000313|Proteomes:UP000000323}; RN [1] {ECO:0000313|EMBL:ACZ43653.1, ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; RX PubMed=21304745; RA Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M., Tice H., RA Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., RA Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.J., Jeffries C.D., Lu M., Brettin T., Detter J.C., Goker M., RA Tindall B.J., Beck B., McDermott T.R., Woyke T., Bristow J., Eisen J.A., RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Cheng J.F.; RT "Complete genome sequence of 'Thermobaculum terrenum' type strain (YNP1)."; RL Stand. Genomic Sci. 3:153-162(2010). RN [2] {ECO:0000313|Proteomes:UP000000323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323}; RX DOI=10.4056/sigs.1153107; RA Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T., Nolan M., RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y., Jeffries C., Lu M., Brettin T., Detter J., Goker M., RA Tindall B., Beck B., McDermott T., Woyke T., Bristow J., Eisen J., RA Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). 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; CP001826; ACZ43653.1; -; Genomic_DNA. DR RefSeq; WP_012876684.1; NC_013526.1. DR AlphaFoldDB; D1CIT3; -. DR STRING; 525904.Tter_2767; -. DR EnsemblBacteria; ACZ43653; ACZ43653; Tter_2767. DR KEGG; ttr:Tter_2767; -. DR eggNOG; COG0108; Bacteria. DR eggNOG; COG0807; Bacteria. DR HOGENOM; CLU_020273_1_2_0; -. DR OMA; ECRGLIC; -. DR OrthoDB; 9793111at2; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000000323; Chromosome 2. 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; 3.90.870.10; DHBP synthase; 1. DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 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 NCBIfam; TIGR00505; ribA; 1. DR NCBIfam; TIGR00506; ribB; 1. DR PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR PIRSF; PIRSF001259; RibA; 1. DR SUPFAM; SSF142695; RibA-like; 1. DR SUPFAM; SSF55821; YrdC/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:UP000000323}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_01283}; Zinc {ECO:0000256|HAMAP-Rule:MF_01283}. FT DOMAIN 215..373 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000259|Pfam:PF00925" FT REGION 1..204 FT /note="DHBP synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 205..407 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 329 FT /note="Proton acceptor; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 331 FT /note="Nucleophile; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 27..28 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 32 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 142..146 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 145 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 166 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 253..257 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 258 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 269 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 271 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 274 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 295..297 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 317 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 352 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 357 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 128 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 166 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" SQ SEQUENCE 407 AA; 44349 MW; F253C847500A2D21 CRC64; MTGSKIQQAL DELRAGRFVV VVDDESRERE ADLVLAAQHA TPAAINFMAR EACGLICVAM HGRRMDQLGI PPMVSPENNT SAHGTAFGVP VDAASGITTG ISAYDRAHTI RLLADPSSTP GDFIMPGHVF PLRAREGGVL ERRGHTEAAV DLMVMAGLQP VAAICEIMAP NGRMAWGEEL EEFAHRHNLM LVTVQEVADA RAAESEGTLG KVRPVKLPTS HGEFTLVAYT APDSREPHLA LIHGDPGSSP LVRLHSECFT GDVLGSERCD CGPQLDRALQ MIAAQGGILL YLRQEGRGIG LLNKLRAYAL QDEGLDTVEA NEHLGFQPDE RDYAVAAEIL RDLGVSSVRL LTNNPRKIEG LRAHGIEVVE RVPLEVPPRR HNLRYLQTKK LKLGHWLQLH PPIGEQR //