ID A0A7W7GN15_9MICC Unreviewed; 617 AA. AC A0A7W7GN15; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 6. DE RecName: Full=GTP cyclohydrolase-2 {ECO:0000256|HAMAP-Rule:MF_00179}; DE EC=3.5.4.25 {ECO:0000256|HAMAP-Rule:MF_00179}; DE AltName: Full=GTP cyclohydrolase II {ECO:0000256|HAMAP-Rule:MF_00179}; GN Name=ribA {ECO:0000256|HAMAP-Rule:MF_00179}; GN ORFNames=HDA30_000666 {ECO:0000313|EMBL:MBB4735158.1}; OS Micrococcus cohnii. OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus. OX NCBI_TaxID=993416 {ECO:0000313|EMBL:MBB4735158.1, ECO:0000313|Proteomes:UP000540191}; RN [1] {ECO:0000313|EMBL:MBB4735158.1, ECO:0000313|Proteomes:UP000540191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 23974 {ECO:0000313|EMBL:MBB4735158.1, RC ECO:0000313|Proteomes:UP000540191}; RA Klenk H.-P.; RT "Sequencing the genomes of 1000 actinobacteria strains."; RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases. 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}. 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_00179}. 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 -!- 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_00179}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00179}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00179}; 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}. 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_00179}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family. CC {ECO:0000256|HAMAP-Rule:MF_00179}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase CC family. {ECO:0000256|ARBA:ARBA00005520}. 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:MBB4735158.1}. 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; JACHNA010000001; MBB4735158.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7W7GN15; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000540191; Unassembled WGS sequence. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC. 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: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 CDD; cd00402; Riboflavin_synthase_like; 1. DR Gene3D; 2.40.30.20; -; 2. DR Gene3D; 3.40.50.10990; -; 1. DR HAMAP; MF_00179; RibA; 1. DR InterPro; IPR023366; ATP_synth_asu-like_sf. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR InterPro; IPR032677; GTP_cyclohydro_II. DR InterPro; IPR001783; Lumazine-bd. DR InterPro; IPR026017; Lumazine-bd_dom. DR InterPro; IPR000926; RibA. DR InterPro; IPR036144; RibA-like_sf. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR Pfam; PF00677; Lum_binding; 2. DR SUPFAM; SSF142695; RibA-like; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 2. DR SUPFAM; SSF55821; YrdC/RibB; 1. DR TIGRFAMs; TIGR00506; ribB; 1. DR PROSITE; PS51177; LUMAZINE_BIND; 2. PE 3: Inferred from homology; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00179}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00179}; KW Lyase {ECO:0000313|EMBL:MBB4735158.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00179}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00179}; Reference proteome {ECO:0000313|Proteomes:UP000540191}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_00179}; Zinc {ECO:0000256|HAMAP-Rule:MF_00179}. FT DOMAIN 1..109 FT /note="Lumazine-binding" FT /evidence="ECO:0000259|PROSITE:PS51177" FT REPEAT 1..109 FT /note="Lumazine-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524" FT DOMAIN 110..211 FT /note="Lumazine-binding" FT /evidence="ECO:0000259|PROSITE:PS51177" FT REPEAT 110..211 FT /note="Lumazine-binding" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00524" FT ACT_SITE 545 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT ACT_SITE 547 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 468..472 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 473 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 484 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 486 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 489 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 511..513 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 533 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 568 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" FT BINDING 573 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00179" SQ SEQUENCE 617 AA; 64562 MW; B364191667E1A242 CRC64; MFTGIITHIG TVVALQQDEQ SDTAVLVLDT AGAAAGLPEG GSLAVNGVCL TSVPQDADPS APDSAPDDGL FRADLMGQTL RMTALGELSP GDRVNLERCL RPTDHIDGHI VQGHVDGVGT VAQVADEGAW RRVRVAVPDE LARVIPAQGA ITVQGVSLTV TAVSAPSQRR HWFEVGLIPA TLEATVLGAL APGDRVNLET DVMARYAERM TQIPSSEPVR LDGVDRAVEQ LAAGRPVIVV DDEDRENEGD IVFAAALATD EVTAFTIRHT SGVLCAPMPG AVADRLELPP MTATNQDPKG TAYTVSVDAA AGVTTGISAA DRARTLRVLA GAQSAPADLT RPGHVFPLRA VDGGVAQRSG HTEAGVELCR LAGLPPVAAI AELTHDDGTM MRLPALRRFA DDHALALISI EDLQAHLSGV DSTEDALLPT KHGQLRVSAH RDAATGVEHV LLRPVEPVGD SGAPDVVRVH SECLTGDAFG SLRCDCGPQL QHALEQTART GGAVLYVRGH EGRGIGLAAK LRAYALQDAG RDTVDANLDL GLPADARDWA GAAAVLRAAG LERIRLVTNN PAKADGLREH GIDIVELLPA PAPVTEHNLA YLRTKRDRMG HTVPGLD //