ID A0A352X952_9CYAN Unreviewed; 556 AA. AC A0A352X952; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 13-FEB-2019, entry version 4. 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=DDW51_13290 {ECO:0000313|EMBL:HBE18551.1}; OS Cyanobacteria bacterium UBA11367. OC Bacteria; Cyanobacteria. OX NCBI_TaxID=2055774 {ECO:0000313|EMBL:HBE18551.1}; RN [1] {ECO:0000313|EMBL:HBE18551.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA11367 {ECO:0000313|EMBL:HBE18551.1}; 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}. 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: 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:HBE18551.1}. 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; DNOY01000287; HBE18551.1; -; 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:HBE18551.1}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01283, ECO:0000313|EMBL:HBE18551.1}; 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 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 221 385 GTP_cyclohydro2. {ECO:0000259|Pfam: FT PF00925}. FT NP_BIND 264 268 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT NP_BIND 307 309 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 1 211 DHBP synthase. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT REGION 35 36 D-ribulose 5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 150 154 D-ribulose 5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 212 556 GTP cyclohydrolase II. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT ACT_SITE 341 341 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT ACT_SITE 343 343 Nucleophile; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 36 36 Magnesium or manganese 1. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 36 36 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 153 153 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 269 269 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 280 280 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 282 282 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT BINDING 40 40 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 174 174 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 285 285 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 329 329 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 364 364 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 369 369 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 136 136 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 174 174 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. SQ SEQUENCE 556 AA; 61819 MW; 068AA2C1E0005EE3 CRC64; MESSETNLFE FDSIDAALED LKAGRALVVV DDENRENEGD LICAAQFATP DMINFMAVEA RGLICLALTG QRLDELDVPL MVSKNTDSNQ TAFTISIDAS THVGVTTGIS AEDRAKTIQV AIDPHTKPSD LRRPGHIFPI RAKEGGVLKR AGHTEAAVDL PRLAGLYPAG VICEIQNLDG SMARLPQLVK YAKYHQLKLI SIADLIGYRL KYDRFVYRES VAKLPSVFGN FEIYGYRNAL DNSEHVAIVK GNPAEFQDNP VMVRMHSECL TGDGLGSLRC DCRMQLEAAL KMIENAGQGV VVYLRQEGRG IGLVNKLKAY SLQDMGLDTV EANERLGFPA DLRDYGMGAQ MLNDIGVQKI RLITNNPRKI AGLRGYGLEV VDRVPLLIES NDYNSTYLAT KAQKLGHLLL QTYLVSVAIH WNDAPEGIEQ RYERLEKIRS LVHSQNLLLQ EESRPVAIAL FDKPSLIVHL GFDQANLAAP DWYKNTQHPY LQAILKILDT LSQWPQVGRL AILISSGIDP LTSLQVRLDR ERLPLTQPPS LICDRLSTQK VYSFDR //