ID A0A0B5HRN8_ARCG5 Unreviewed; 398 AA.
AC A0A0B5HRN8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=GTP cyclohydrolase II {ECO:0000256|ARBA:ARBA00012762};
DE EC=3.5.4.25 {ECO:0000256|ARBA:ARBA00012762};
GN ORFNames=QT03_C0001G1370 {ECO:0000313|EMBL:AJF60847.1};
OS Archaeon GW2011_AR10.
OC Archaea.
OX NCBI_TaxID=1579370 {ECO:0000313|EMBL:AJF60847.1, ECO:0000313|Proteomes:UP000031777};
RN [1] {ECO:0000313|Proteomes:UP000031777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25702576; DOI=10.1016/j.cub.2015.01.014;
RA Castelle C.J., Wrighton K.C., Thomas B.C., Hug L.A., Brown C.T.,
RA Wilkins M.J., Frischkorn K.R., Tringe S.G., Singh A., Markillie L.M.,
RA Taylor R.C., Williams K.H., Banfield J.F.;
RT "Genomic expansion of domain archaea highlights roles for organisms from
RT new phyla in anaerobic carbon cycling.";
RL Curr. Biol. 25:690-701(2015).
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};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004853}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC family. {ECO:0000256|ARBA:ARBA00005520}.
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DR EMBL; CP010424; AJF60847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5HRN8; -.
DR STRING; 1579370.QT03_C0001G1370; -.
DR KEGG; agw:QT03_C0001G1370; -.
DR HOGENOM; CLU_020273_1_2_2; -.
DR UniPathway; UPA00275; UER00400.
DR Proteomes; UP000031777; Chromosome.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.90.870.10; DHBP synthase; 1.
DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 1.
DR HAMAP; MF_00179; RibA; 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 NCBIfam; TIGR00505; ribA; 1.
DR NCBIfam; TIGR00506; ribB; 1.
DR PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR Pfam; PF00926; DHBP_synthase; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR PIRSF; PIRSF001259; RibA; 1.
DR SUPFAM; SSF142695; RibA-like; 1.
DR SUPFAM; SSF55821; YrdC/RibB; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AJF60847.1};
KW Lyase {ECO:0000313|EMBL:AJF60847.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619}.
FT DOMAIN 207..374
FT /note="GTP cyclohydrolase II"
FT /evidence="ECO:0000259|Pfam:PF00925"
SQ SEQUENCE 398 AA; 44041 MW; 1AEAC7CECE0DF7B3 CRC64;
METKFNSIEE ASRELKSGKL VVLVDDEHRE NEGDLVLAAE LASEEKINFI IKEARGLMCI
PITEGKAAQL GLRKMIENTD RFETPFTVSV DAKTASTGVS VKDRLKTINA IVSDSTVPEE
LVKPGHLFPL VSKKGGVLHR AGHTEGAIDL MKIAVLKPVA VIAEIMNDDG SMARLPDLLK
FREKHGLMIV ALKDLIRYRL KEESLIERVA ATSIPTEFGA FEAVGFKDKV YGEEYIALVK
GKVSGEKNVL VRVHSGCLTG DVFHSHRCDC NAQLHESLRV IEREGKGALL YIMHHEGRGI
GLLNKLKAYE LQDKGLDTVE ANLKLGFKMD ERDYGIGAQI LRELGLTSIR LLTNNPKKLS
ALKGYGLEVT EMVPIKTTPT TFNKSYLLTK KQKMGHLL
//
