ID D2QU60_SPILD Unreviewed; 432 AA. AC D2QU60; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 14-DEC-2022, entry version 90. 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=Slin_6384 {ECO:0000313|EMBL:ADB42342.1}; OS Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896). OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae; OC Spirosoma. OX NCBI_TaxID=504472 {ECO:0000313|EMBL:ADB42342.1, ECO:0000313|Proteomes:UP000002028}; RN [1] {ECO:0000313|Proteomes:UP000002028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896 RC {ECO:0000313|Proteomes:UP000002028}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., RA Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S., RA Goker M., Klenk H.-P., Eisen J.A.; RT "The complete chromosome of Spirosoma linguale DSM 74."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADB42342.1, ECO:0000313|Proteomes:UP000002028} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33905 / DSM 74 / LMG 10896 RC {ECO:0000313|Proteomes:UP000002028}; RX PubMed=21304700; RA Lail K., Sikorski J., Saunders E., Lapidus A., Glavina Del Rio T., RA Copeland A., Tice H., Cheng J.-F., Lucas S., Nolan M., Bruce D., RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G., RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J., RA Jeffries C.D., Chain P., Brettin T., Detter J.C., Schuetze A., Rohde M., RA Tindall B.J., Goeker M., Bristow J., Eisen J.A., Markowitz V., RA Hugenholtz P., Kyrpides N.C., Klenk H.-P., Chen F.; RT "Complete genome sequence of Spirosoma linguale type strain (1)."; RL Stand. Genomic Sci. 2:176-185(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; CP001769; ADB42342.1; -; Genomic_DNA. DR AlphaFoldDB; D2QU60; -. DR STRING; 504472.Slin_6384; -. DR EnsemblBacteria; ADB42342; ADB42342; Slin_6384. DR KEGG; sli:Slin_6384; -. DR eggNOG; COG0108; Bacteria. DR eggNOG; COG0807; Bacteria. DR HOGENOM; CLU_020273_1_2_10; -. DR OMA; ECRGLIC; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000002028; 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; RibA-like; 1. DR SUPFAM; SSF55821; YrdC/RibB; 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}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_01283}; Zinc {ECO:0000256|HAMAP-Rule:MF_01283}. FT DOMAIN 236..398 FT /note="GTP_cyclohydro2" FT /evidence="ECO:0000259|Pfam:PF00925" FT REGION 1..226 FT /note="DHBP synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 227..432 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT COMPBIAS 1..20 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 354 FT /note="Proton acceptor; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 356 FT /note="Nucleophile; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 51..52 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 52 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 56 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 165..169 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 168 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 189 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 277..281 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 282 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 293 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 295 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 298 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 320..322 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 342 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 377 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 382 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 151 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 189 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" SQ SEQUENCE 432 AA; 47621 MW; 2103DF9F08ED4892 CRC64; MMSNNSTNSE INSANEENPA ESNPIRLDRI EDAIADIKAG KIVLVVDDED RENEGDMICA AEMITPEMVN FMVREARGLM CAPLTQERCD ELGLDMMVTS NTSVHTTPFT VSVDLLGNGC TTGISASDRS KTIQALVDPN TTPDDLGRPG HIFPLRAVEG GVIRRAGHTE AAVDLAKLAG LSPVGVLIEV LNEDGTMARL PELRVLADRF GMRLVSIQDL IAYRLRTETL IRREIGVDMP TQWGHFDLIA YKQSNTGDTH LALVKGTWEP NEPVMVRVHS SCVTGDIFGS CRCDCGPQLH AAMELVEKEG KGVVVYMFQE GRGIGLINKL KAYKLQEMGR DTVEANLDLG LPMDARDYGV GAQILRDLGI RKLRLISNNP KKRAGLMGYG LEIVDTVPLE IKSNPHNERY LRTKRDKMGH TIMNEPVNEE QE //