ID A0A3D5WAT2_9DELT Unreviewed; 401 AA. AC A0A3D5WAT2; DT 16-JAN-2019, integrated into UniProtKB/TrEMBL. DT 16-JAN-2019, sequence version 1. DT 05-JUN-2019, entry version 5. 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=DHT43_00080 {ECO:0000313|EMBL:HCX88922.1}; OS Deltaproteobacteria bacterium. OC Bacteria; Proteobacteria; Deltaproteobacteria. OX NCBI_TaxID=2026735 {ECO:0000313|EMBL:HCX88922.1}; RN [1] {ECO:0000313|EMBL:HCX88922.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA8473 {ECO:0000313|EMBL:HCX88922.1}; RX PubMed=30148503; DOI=.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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:SAAS01116086}; 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01283}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HCX88922.1}. 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; DPPR01000003; HCX88922.1; -; Genomic_DNA. DR UniPathway; UPA00275; UER00399. 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|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:HCX88922.1}; 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:SAAS00434439}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01283}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00711707}; KW Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000256|SAAS:SAAS00434473}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000256|SAAS:SAAS00711685}. FT DOMAIN 208 374 GTP_cyclohydro2. {ECO:0000259|Pfam: FT PF00925}. FT NP_BIND 253 257 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT NP_BIND 296 298 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 1 201 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 202 401 GTP cyclohydrolase II. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT ACT_SITE 330 330 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT ACT_SITE 332 332 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 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 164 164 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 274 274 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 318 318 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 353 353 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 358 358 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 126 126 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 164 164 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. SQ SEQUENCE 401 AA; 44579 MW; CC8A0C5D34877DD4 CRC64; MALSTIKEAI EDIKKGKIII LVDDEDRENE GDLMMAAEKI TPDAVNFMAR YGRGLICLTL NEKRAKELHL SPMVTDNTSH FNTAFTVSIE ARCGVTTGIS AADRAMTILT AIDEKTKPQD LARPGHIFPI IARNGGVLVR TGQTEGSVDL ARLSGLIPAG VICEIMKDDG TMARMPDLEI FAEKHGLKIV TIADIIEYRL QNEGLVRRVA ETRIPTLYGG EFKAIAYEND VDSHQHLALV KGDINPEDEI LVRVHSECLT GDVFGSQRCD CGEQLHTAMR MIEEEGKGVI VYMHQEGRGI GLINKLRAYE LQDQGLDTVQ ANERLGFKPD LRDYGVGAQI LRDLGVRKMR QMTNNPKKIK GIEGYGLVVT ERVPIETKPN DNNIKYLETK KKKMGHMLNI K //