ID A0A292DDN0_STALU Unreviewed; 393 AA. AC A0A292DDN0; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 12-AUG-2020, entry version 16. 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=EQ812_09590 {ECO:0000313|EMBL:TBW71722.1}; OS Staphylococcus lugdunensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=28035 {ECO:0000313|EMBL:TBW71722.1, ECO:0000313|Proteomes:UP000293637}; RN [1] {ECO:0000313|EMBL:TBW71722.1, ECO:0000313|Proteomes:UP000293637} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E7 {ECO:0000313|EMBL:TBW71722.1, RC ECO:0000313|Proteomes:UP000293637}; RA Williams M.R.; RT "Quorum sensing between bacterial species on the skin protects against RT epidermal injury in atopic dermatitis."; RL Sci. Transl. Med. 0:0-0(2019). 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 + 3 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)- CC pyrimidine + diphosphate + formate + 2 H(+); Xref=Rhea:RHEA:23704, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:58614; EC=3.5.4.25; CC Evidence={ECO:0000256|ARBA:ARBA00000698, 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; 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TBW71722.1}. 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; SCHB01000006; TBW71722.1; -; Genomic_DNA. DR RefSeq; WP_002478008.1; NZ_SCHB01000006.1. DR GeneID; 29732768; -. DR OrthoDB; 900513at2; -. DR UniPathway; UPA00275; UER00400. DR Proteomes; UP000293637; Unassembled WGS sequence. 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|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_01283}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01283, KW ECO:0000313|EMBL:TBW71722.1}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, 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}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP- KW 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 NP_BIND 249..253 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT NP_BIND 291..293 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 1..200 FT /note="DHBP synthase" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 27..28 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 139..143 FT /note="D-ribulose 5-phosphate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT REGION 201..393 FT /note="GTP cyclohydrolase II" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 325 FT /note="Proton acceptor; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT ACT_SITE 327 FT /note="Nucleophile; for GTP cyclohydrolase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 28 FT /note="Magnesium or manganese 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 28 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 142 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 254 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 265 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT METAL 267 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 32 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 163 FT /note="D-ribulose 5-phosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 270 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 313 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 348 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT BINDING 353 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 125 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" FT SITE 163 FT /note="Essential for DHBP synthase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01283" SQ SEQUENCE 393 AA; 44308 MW; ADDA817CFEDA4288 CRC64; MQFDTIEEAL QALKKGETII VVDDEDRENE GDLVAVTQWM QDQTINFMAK HGRGLICTPI STDIAERLEL KPMVMQNSDD YGTNFTVSID HYTTTTGISA IERMTTARSL IATDTMAEDF HKPGHLFPLI AKDNGVLERE GHTEATVDLA KMTGAAPAGV ICEIMNDDGS MAKGEQLEKF KETHQLKLIS IKQIIEYRHQ HDIQVNLRAK VNMPTDFGNF EMYGFDSTLT QDEIVVITKG EPRTTENVRI HSACLTGDIF HSQRCDCGAQ LESSLKYINE HGGMVIYLPQ EGRGIGLINK LRAYELIEQG YDTVTANLAL GFDEDLRDYK VASQILKYFN VKQVNLLSNN PKKFEGLSEY DIEIAKRIEV IVPETTHNHD YMETKKIKMG HLI //