ID A0A292DDN0_STALU Unreviewed; 393 AA. AC A0A292DDN0; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 05-JUN-2019, entry version 11. 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=B6N54_05555 {ECO:0000313|EMBL:ARJ16067.1}, B6N84_05570 GN {ECO:0000313|EMBL:ARJ29462.1}, B7469_03245 GN {ECO:0000313|EMBL:ARJ26725.1}, CRN64_00230 GN {ECO:0000313|EMBL:ATN13890.1}; OS Staphylococcus lugdunensis. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=28035 {ECO:0000313|EMBL:ATN13890.1, ECO:0000313|Proteomes:UP000224250}; RN [1] {ECO:0000313|Proteomes:UP000242207, ECO:0000313|Proteomes:UP000242698, ECO:0000313|Proteomes:UP000243403} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C_33 {ECO:0000313|EMBL:ARJ26725.1, RC ECO:0000313|Proteomes:UP000242698}, VISLISI_27 RC {ECO:0000313|EMBL:ARJ16067.1, ECO:0000313|Proteomes:UP000243403}, and RC VISLISI_33 {ECO:0000313|EMBL:ARJ29462.1, RC ECO:0000313|Proteomes:UP000242207}; RX PubMed=28444231; RA Argemi X., Martin V., Loux V., Dahyot S., Lebeurre J., Guffroy A., RA Martin M., Velay A., Keller D., Riegel P., Hansmann Y., Paul N., RA Prevost G.; RT "Whole genome sequencing of 7 strains of Staphylococcus lugdunensis RT allows identification of mobile genetic elements."; RL Genome Biol. Evol. 0:0-0(2017). RN [2] {ECO:0000313|EMBL:ATN13890.1, ECO:0000313|Proteomes:UP000224250} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_381 {ECO:0000313|EMBL:ATN13890.1, RC ECO:0000313|Proteomes:UP000224250}; RA Goldberg B., Campos J., Tallon L., Sadzewicz L., Ott S., Zhao X., RA Nagaraj S., Vavikolanu K., Aluvathingal J., Nadendla S., Geyer C., RA Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx RT tests."; RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases. 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 --------------------------------------------------------------------------- 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; CP020735; ARJ16067.1; -; Genomic_DNA. DR EMBL; CP020768; ARJ26725.1; -; Genomic_DNA. DR EMBL; CP020769; ARJ29462.1; -; Genomic_DNA. DR EMBL; CP023970; ATN13890.1; -; Genomic_DNA. DR RefSeq; WP_002478008.1; NZ_SCHB01000006.1. DR GeneID; 29732768; -. DR OrthoDB; 900513at2; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000224250; Chromosome. DR Proteomes; UP000242207; Chromosome. DR Proteomes; UP000242698; Chromosome. DR Proteomes; UP000243403; 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; 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:UP000224250, KW ECO:0000313|Proteomes:UP000242207, ECO:0000313|Proteomes:UP000242698, KW ECO:0000313|Proteomes:UP000243403}; 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:ATN13890.1}; 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 209 368 GTP_cyclohydro2. {ECO:0000259|Pfam: FT PF00925}. FT NP_BIND 249 253 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT NP_BIND 291 293 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 1 200 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 139 143 D-ribulose 5-phosphate binding. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT REGION 201 393 GTP cyclohydrolase II. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT ACT_SITE 325 325 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT ACT_SITE 327 327 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 142 142 Magnesium or manganese 2. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT METAL 254 254 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 265 265 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01283}. FT METAL 267 267 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 163 163 D-ribulose 5-phosphate. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 270 270 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 313 313 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 348 348 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT BINDING 353 353 GTP. {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 125 125 Essential for DHBP synthase activity. FT {ECO:0000256|HAMAP-Rule:MF_01283}. FT SITE 163 163 Essential for DHBP synthase activity. FT {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 //