ID D1CIT3_THET1 Unreviewed; 407 AA. AC D1CIT3; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 05-DEC-2018, entry version 74. 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; 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., RA Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N., RA Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T., RA Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R., RA Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Cheng J.F.; RT "Complete genome sequence of 'Thermobaculum terrenum' type strain RT (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., RA Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K., RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A., RA Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M., RA Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T., RA Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., RA Kyrpides N., Klenk H., Cheng J.; RT "Complete genome sequence of Thermobaculum terrenum type strain RT (YNP1T)."; RL Stand. Genomic Sci. 3:153-162(2010). 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:SAAS00739193}. 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 CC phosphate + formate + H(+); Xref=Rhea:RHEA:18457, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, CC ChEBI:CHEBI:58830; EC=4.1.99.12; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01283}; CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + 3 H2O = 2,5-diamino-6-hydroxy-4-(5- CC phosphoribosylamino)-pyrimidine + diphosphate + formate + 2 CC H(+); Xref=Rhea:RHEA:23704, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58614; EC=3.5.4.25; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01283, CC ECO:0000256|SAAS:SAAS00711742}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01283}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01283}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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: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, ECO:0000256|SAAS:SAAS00711724}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000256|HAMAP-Rule:MF_01283, CC ECO:0000256|SAAS:SAAS00789992}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000256|HAMAP-Rule:MF_01283, CC ECO:0000256|SAAS:SAAS00534513}. 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 STRING; 525904.Tter_2767; -. DR EnsemblBacteria; ACZ43653; ACZ43653; Tter_2767. DR KEGG; ttr:Tter_2767; -. DR eggNOG; ENOG4105C66; Bacteria. DR eggNOG; COG0108; LUCA. DR eggNOG; COG0807; LUCA. DR HOGENOM; HOG000115440; -. DR KO; K14652; -. DR OMA; GCTTGIS; -. DR OrthoDB; POG091H008U; -. DR BioCyc; TTER525904:G1GGS-2813-MONOMER; -. 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; 3.40.50.10990; -; 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 Complete proteome {ECO:0000313|Proteomes:UP000000323}; KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00711691}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS01033620, ECO:0000313|EMBL:ACZ43653.1}; 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:SAAS00037896}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00711707}; KW Reference proteome {ECO:0000313|Proteomes:UP000000323}; KW Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00037880}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711685}. FT DOMAIN 215 373 GTP_cyclohydro2. {ECO:0000259|Pfam: FT PF00925}. FT NP_BIND 253 257 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT NP_BIND 295 297 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 1 204 DHBP synthase. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT REGION 27 28 D-ribulose 5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 142 146 D-ribulose 5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 205 407 GTP cyclohydrolase II. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT ACT_SITE 329 329 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT ACT_SITE 331 331 Nucleophile; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 28 28 Magnesium or manganese 1. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 28 28 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 145 145 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 258 258 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 269 269 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 271 271 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT BINDING 32 32 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 166 166 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 274 274 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 317 317 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 352 352 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 357 357 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 128 128 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 166 166 Essential for DHBP synthase activity. FT {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 //